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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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=
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+
molybdate-[molybdate-binding protein][side 1]
=
+
+
+
[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
-
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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-
-
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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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-
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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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-
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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]
-
-
-
-
?
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
-
-
-
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
-
-
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
-
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
enzyme is involved in molybdate transport
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
import of molybdate
-
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
-
-
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
-
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
-
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
-
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
-
-
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
the ATPase activity is strictly required
-
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Oleidesulfovibrio alaskensis
-
-
-
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Oleidesulfovibrio alaskensis G20
-
-
-
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
import of molybdate
-
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
-
-
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
enzyme is involved in molybdate transport
-
?
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
-
-
?
additional information
?
-
-
ModABC can also transport tungstate and sulfate. ModA specifically binds molybdate or tungstate
-
-
?
additional information
?
-
-
the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
-
-
?
additional information
?
-
the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
-
-
?
additional information
?
-
-
ModABC can also transport tungstate
-
-
?
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
-
-
?
additional information
?
-
-
the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
-
-
?
additional information
?
-
the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
-
-
?
additional information
?
-
-
ModABC can also transport tungstate and sulfate. ModA specifically binds molybdate or tungstate, WtpABC transports tungstate and molybdate in Pyrococcus furiosus
-
-
?
additional information
?
-
-
WtpABC transports tungstate and molybdate in Pyrococcus furiosus, overview
-
-
?
additional information
?
-
-
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
-
additional information
-
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
-
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
Molybdate transporter ModABC is important for Pseudomonas aeruginosa chronic lung infection.
Starvation
Molybdate transport and its effect on nitrogen utilization in the cyanobacterium Anabaena variabilis ATCC 29413.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
0.000025-0.000050 mM, molybdate, pH 7.0
-
additional information
additional information
Oleidesulfovibrio alaskensis
-
oxoanion binding kinetic of ModA, overview
-
additional information
additional information
-
transporter component interaction kinetics and affinities, overview
-
additional information
additional information
transporter component interaction kinetics and affinities, overview
-
additional information
additional information
-
transporter component interaction kinetics and affinities, overview
-
additional information
additional information
transporter component interaction kinetics and affinities, overview
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene modA; harbors genes modABC, no tupABC genes
UniProt
brenda
gene modB; harbors genes modABC, no tupABC genes
UniProt
brenda
gene modC; harbors genes modABC, no tupABC genes
UniProt
brenda
gene modA; harbors genes modABC, no tupABC genes
UniProt
brenda
gene modB; harbors genes modABC, no tupABC genes
UniProt
brenda
gene modC; harbors genes modABC, no tupABC genes
UniProt
brenda
ModABC transporter is encoded by the modABC operon, gene modA encodes the molybdate-binding protein ModA, ModC is encoded by the modC gene and is the ATPase subunit
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
high expression level, expression in the protodermal cells behind the root tip, and in epidermis and cortex at the elongation zone
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
MOT1 contains an N-terminal mitochondrial targeting sequence
brenda
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ModB and ModC, ModB possesses six transmembrane domains
brenda
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ModB and ModC, ModB possesses six transmembrane domains
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transmembrane domain structure, overview
brenda
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ModB is a integral membrane, channel-forming protein
brenda
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ModB is a integral membrane, channel-forming protein
brenda
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ModB and ModC, ModB possesses six transmembrane domains
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
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ModABC belongs to the family of ATP-binding cassette (ABC) transporters, while PerO is a member of the ArsB/NhaD family
evolution
-
ModABC belongs to the family of molybdate uptake transporters MolT
evolution
-
ModABC belongs to the family of molybdate uptake transporters MolT
evolution
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ModABC belongs to the family of molybdate uptake transporters MolT
evolution
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ModABC belongs to the family of molybdate uptake transporters MolT
evolution
-
ModABC belongs to the family of molybdate uptake transporters MolT, PerO belongs to the ArsB/NhaD ion transporter family
evolution
-
WtpABC belongs to the sulfate/tungstate uptake transporter SulT family, overview. ModABC belongs to the family of molybdate uptake transporters MolT
evolution
-
WtpABC belongs to the sulfate/tungstate uptake transporter SulT family, overview. ModABC belongs to the family of molybdate uptake transporters MolT
malfunction
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during growth under Mo-replete conditions, the wild-type strain accumulates considerably more Mo than the enzyme mutant
malfunction
-
an enzyme mutation is sufficient to prevent growth on nitrate without the addition of molybdate to the growth medium
malfunction
-
an enzyme mutation is sufficient to prevent growth on nitrate without the addition of molybdate to the growth medium
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metabolism
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Campylobacter jejuni possesses a specific, ultra high affinity tungstate transporter that supplies tungsten for incorporation into formate dehydrogenase, in additon to a molybdate/tungstate transporter ModA, EC 3.6.3.29, and also two MoeA paralogues which may explain the formation of both molybdopterin and tungstopterin in this bacterium
metabolism
-
ModE-like protein regulates both transporters, repressing mod in the presence of both molybdenum and tungsten and tup only in the presence of tungsten. Like other ModE proteins, the Campylobacter jejuni ModE binds DNA through a helix-turn-helix DNA binding domain, but unlike other members of the ModE family it does not have a metal binding domain
metabolism
specific high-affinity ATP-binding cassette (ABC) transporting systems uptake molybdenum and tungsten in the form of soluble oxyanions, molybdate and tungstate. Among them are the bacterial TupABC transporting system, which is highly specific for tungstate and does not transport other anions, and the ModABC system, which can transport both molybdate and tungstate, regulation of the ModABC transport system. TunR proteins participate in protection of the cells from the inhibition by these oxyanions
metabolism
-
specific high-affinity ATP-binding cassette (ABC) transporting systems uptake molybdenum and tungsten in the form of soluble oxyanions, molybdate and tungstate. Among them are the bacterial TupABC transporting system, which is highly specific for tungstate and does not transport other anions, and the ModABC system, which can transport both molybdate and tungstate, regulation of the ModABC transport system. TunR proteins participate in protection of the cells from the inhibition by these oxyanions
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physiological function
-
molybdenum is typically transported into the cell via an ABC type transport system encoded by the modABC operon. The modA gene codes for the periplasmic binding protein, modB codes for the transmembrane protein, and modC codes for an ATP-binding protein. The enzyme provides molybdenum or tungsten for incorporation into the format dehydrogenase, formate dehydrogenase is active in the presence of either tungsten or molybdenum
physiological function
-
ModA is responsible for metal binding and ATPase hydrolysis, ModB functions as a homodimer to form the channel for molybdate transport
physiological function
-
ModA is responsible for metal binding and ATPase hydrolysis, ModB functions as a homodimer to form the channel for molybdate transport
physiological function
-
ModA is responsible for metal binding and ATPase hydrolysis, ModB functions as a homodimer to form the channel for molybdate transport
physiological function
-
ModA is responsible for metal binding and ATPase hydrolysis, ModB functions as a homodimer to form the channel for molybdate transport
physiological function
-
ModA is responsible for metal binding and ATPase hydrolysis, ModB functions as a homodimer to form the channel for molybdate transport. ATPase ModC from Methanosarcina acetivorans possesses a regulatory domain
physiological function
-
ModA is responsible for metal binding, ModB functions as a homodimer to form the channel for molybdate transport, ModC is the ATPase subunit of the ModABC complex that energizes molybdate transport. Regulation of the modABC operon by the molybdate-responsive ModE protein, overview. The active form of ModE, which binds to the modA operator, is the ModE-molybdate complex, interaction between the modA operator and ModE-Mo
physiological function
-
ModABC consists of the ModA periplasmic solute-binding protein, the integral membrane-transport protein ModB and the ATP-binding and hydrolysis cassette protein ModC
physiological function
-
ModABC imports molybdate in nanomolar range into the cell, another oxyanion permease, PerO, which is a general oxyanion importer, also imports molybdate in the micromolar range, overview. PerO is involved in molybdenum accumulation, but PerO is dispensable under standard growth conditions
physiological function
-
periplasmic binding protein MolA delivers substrate to the ABC transporter MolB2C2
physiological function
afModBCA is a high-affinity transport system for molybdate and tungstate anions
physiological function
regulator family, tungstate-responsive regulator (TunR) controls the homeostasis of tungstate and molybdate in sulfate-reducing delta-proteobacteria, activation of modA and modBC genes by TunR in Desulfovibrio vulgaris in vivo by a ModE-like regulatory mechanism
physiological function
Oleidesulfovibrio alaskensis
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the ModABC system is involved in the cellular uptake of molybdate and belongs to the ABC (ATP binding cassette)-type transporter systems. The ModA component is a periplasmic protein that binds molybdate anions, which are then transported through the membrane by the ModB component using ATP hydrolysis as the energy source, the reaction is catalyzed by the ModC component. The genes encoding the three components are organized in an operon modABC regulated by a transcription factor known as ModE. Under an excess of molybdate, ModE binds molybdate ions, suffers conformational changes and dimerizes. This metal-protein complex binds to a specific DNA sequence (located upstream of the modABC operon) and downregulates the expression of proteins involved in molybdenum uptake. Under oxoanion starvation, the component A binds molybdate and interacts with the component B to actively transport molybdate or tungstate from the periplasm to the cytoplasm. The ModABC transport system and, more specifically, the component A may constitute the first selection gate from which cells differentiate between Mo and W. Regulation of the transport enzyme complex, overview
physiological function
-
the enzyme is able to scavenge molybdate from the growth medium
physiological function
Oleidesulfovibrio alaskensis G20
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the ModABC system is involved in the cellular uptake of molybdate and belongs to the ABC (ATP binding cassette)-type transporter systems. The ModA component is a periplasmic protein that binds molybdate anions, which are then transported through the membrane by the ModB component using ATP hydrolysis as the energy source, the reaction is catalyzed by the ModC component. The genes encoding the three components are organized in an operon modABC regulated by a transcription factor known as ModE. Under an excess of molybdate, ModE binds molybdate ions, suffers conformational changes and dimerizes. This metal-protein complex binds to a specific DNA sequence (located upstream of the modABC operon) and downregulates the expression of proteins involved in molybdenum uptake. Under oxoanion starvation, the component A binds molybdate and interacts with the component B to actively transport molybdate or tungstate from the periplasm to the cytoplasm. The ModABC transport system and, more specifically, the component A may constitute the first selection gate from which cells differentiate between Mo and W. Regulation of the transport enzyme complex, overview
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physiological function
-
the enzyme is able to scavenge molybdate from the growth medium
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physiological function
-
regulator family, tungstate-responsive regulator (TunR) controls the homeostasis of tungstate and molybdate in sulfate-reducing delta-proteobacteria, activation of modA and modBC genes by TunR in Desulfovibrio vulgaris in vivo by a ModE-like regulatory mechanism
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additional information
-
ModC is negatively regulated by the ranscription factors MopA and MopB, overview
additional information
-
the cellular tungsten content in a cj0303c (modA) mutant is only slightly lower compared to the wild-type enzyme
Show AA Sequence and Transmembrane Helices (1954 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homohexamer
monomer
additional information
?
Oleidesulfovibrio alaskensis G20
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x * 29000, recombinant enzyme, SDS-PAGE
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additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
archaeal ModA proteins possess octahedral coordination, structure of the ModAB2C2 complex, overview. A single ModA protein with the molybdate oxyanion bound to the external side of a ModB2C2 complex. Molybdate or tungstate oxyanions are bound in a cleft between two lobes in ModA. Both lobes interact with ModB and there are several charged residues localized on the interface
additional information
-
the enzyme components afModBC have 12 transmembrane alpha-helices that adopt the characteristic fold of type I ABC importers
additional information
the enzyme components afModBC have 12 transmembrane alpha-helices that adopt the characteristic fold of type I ABC importers
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
bacterial ModA proteins possess tetrahedral coordination
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
molybdenum is typically transported into the cell via an ABC type transport system encoded by the modABC operon. The modA gene codes for the periplasmic binding protein, modB codes for the transmembrane protein, and modC codes for an ATP-binding protein. Campylobacter jejuni encodes an uncharacterized molybdenum transport system including modABC in addition to a unique gene Cj0302c with unknown function
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
the ModB protein has a molecular weight of 24000 Da, the ModC protein has a calculated molecular weight of 39045 Da
additional information
-
ModA is the periplasmic molybdate-binding protein, ModC is a ATP-binding protein
additional information
-
bacterial ModA proteins possess tetrahedral coordination
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
structure of MolA falls into the cluster A of a class III periplasmic binding protein with two topologically similar globular domains, domain I and II correspond to residues 1-175 and 197-322, respectively, MolA topology and binding coordination, overview
additional information
-
the 20 transmembrane alpha-helices of enzyme components hiMolBC present a type II fold
additional information
the 20 transmembrane alpha-helices of enzyme components hiMolBC present a type II fold
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
the regulatory domains of the nucleotide-binding pockets are in close contact and provide two oxyanion pockets at the shared interface, structure analysis and comparison
additional information
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the regulatory domains of the nucleotide-binding pockets are in close contact and provide two oxyanion pockets at the shared interface, structure analysis and comparison
additional information
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archaeal ModA proteins possess octahedral coordination, structure of the ModABC complex, overview
additional information
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ModABC consists of the ModA periplasmic solute-binding protein, the integral membrane-transport protein ModB and the ATP-binding and hydrolysis cassette protein ModC. Bilobal domain structure of ModA with two mixed alpha/beta domains linked by a hinge region and with a deep cleft between the two domains. Upon binding ligand one domain is rotated towards the other by a hinge-bending motion analogously to the Venus flytrap model of bacterial-type periplasmic binding proteins
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
ModA is the periplasmic molybdate-binding protein, ModC is a ATP-binding protein
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
archaeal ModA proteins possess octahedral coordination
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
bacterial ModA proteins possess tetrahedral coordination
additional information
-
binding protein ModA of the molybdate transport system is a lipoprotein, ModB is a integral membrane, channel-forming protein, ModC is the ATP-binding energizer
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
-
bacterial ModA proteins possess tetrahedral coordination
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
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binding protein ModA of the molybdate transport system is a lipoprotein
no modification
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ModA/WtpA molybdate- or tungstate-binding protein crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds
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ModA crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds
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ModA crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds
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MolA bound to tungstate and molybdate, X-ray diffraction structure determination and analysis at 1.6 A resolution
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enzyme in trans-inhibited state, X-ray diffraction structure determination and analysis at A resolution
ModA in the apoprotein conformation and in the molybdate-bound conformation, by sitting-drop and hanging-drop vapor-diffusion methods, mixing of 0.001 ml of protein solution containing 16-23 mg/ml protein with 0.001 ml reservoir solution, containing 1.4 M ammonium citrate pH 6.4 or 1.4 M ammonium citrate pH 6.0, 4 mM sodium sulfate for the apo-protein and 2.1 M ammonium sulfate and either 1% v/v or 3% v/v 2-propanol, and 4% v/v 2.4 M ammonium sulfate for the molybdate-bound protein, equilibration against 100 ml reservoir solution at room temperature for apo-odA and at 293 K for molybdate-bound ModA, 1 week, method optimization, X-ray diffraction structure determination and analysis of apo- and molybdate-bound-ModA at 1.95 A and 1.69 A resolution and at 2.25 A and 2.45 A resolutionm, respectively, molecular replacemen fails, usage of heavy metal labeling instead
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ModA/WtpA molybdate- or tungstate-binding protein crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds
ModA crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds
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ModA/WtpA molybdate- or tungstate-binding protein crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds
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ModA/WtpA molybdate- or tungstate-binding protein crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
transposon Tn5-B22 mutagenesis, the disruption of modB, encoding the permease component of a high-affinity molybdate transporter, lead to impaired As(III) oxidation, phenotype and complementation by mod operon expression, overview
additional information
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transposon Tn5-B22 mutagenesis, the disruption of modB, encoding the permease component of a high-affinity molybdate transporter, lead to impaired As(III) oxidation, phenotype and complementation by mod operon expression, overview
additional information
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construction of T-DNA insertion mutants of Arabidopsis thaliana MOT1, Mo concentrations in shoots of the mot1-1 and mot1-2 mutant plants are reduced to 10% and 20%, respectively, of that in the wild-type, and, in roots, the Mo concentrations are reduced to 20% and 25% of that in the wild-type, phenotype, overview. Molybdate uptake by MOT1 in transformed yeast is not affected by coexistent sulfate, and MOT1 does not complement a sulfate transporter-deficient yeast mutant strain
additional information
-
a naturally occuring deletion mutation in the MOT1 promoter, leading to the mutants Ler-0 and Van-0, is strongly associated with low shoot molybdenum, occurring in seven of the accessions with the lowest shoot content of molybdenum. Consistent with the low molybdenum phenotype, MOT1 expression in low molybednum accessions is reduced, phenotype, overview
additional information
-
ModA and ModB mutant strains, unable to grow aerobically with nitrate as nitrogen source or as respiratory substrate, respectively, and lack nitrate reductase activity, addition of molybdate fully restores wild-type phenotype, amount of molybdate required for suppression of the mutant phenotype is dependent on sulphate concentration
additional information
-
ModA and ModB mutant strains, unable to grow aerobically with nitrate as nitrogen source or as respiratory substrate, respectively, and lack nitrate reductase activity, addition of molybdate fully restores wild-type phenotype, amount of molybdate required for suppression of the mutant phenotype is dependent on sulphate concentration
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additional information
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construction of modA and modA/tupB defective mutants. When both transport systems are disrupted, formate dehydrogenase activity falls to 5% of the wild-type level, but activity is restored to near wild-type levels only with addition of 1 mM Na2WO4, supplementation with 1 mM Na2MoO4 only restores 20% of formate dehydrogenase activity
additional information
-
substituting either Lys, Leu or Glu for Arg-6 using site-directed mutagenesis, positive charge of ARg-6, located in the conserved SARN region of Mop, is not directly involved in oxyanion binding
additional information
-
substituting either Lys, Leu or Glu for Arg-6 using site-directed mutagenesis, positive charge of ARg-6, located in the conserved SARN region of Mop, is not directly involved in oxyanion binding
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additional information
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generation of molybdate transporter mutants by random transposon Tn5 mutagenesis, phenotypes, overview. The mutants grow much better than the wild-type in the presence of 10 mM molybdate, at low Mo concentrations, mutant strains grow as well as the wild-type
additional information
-
mutants in ModA or ModBC, impaired in the transport of molybdate at low concentrations of the anion, but not at high concentrations, unable to grow using nitrate or Mo-nitrogenase, growth using the alternative V-nitrogenase is not impaired in the mutants
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged ModA from Escherichia coli strain BL21-Gold (DE3) by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged ModA in Escherichia coli strain BL21-Gold (DE3)
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gene mot1, quantitative expression analysis by RT-PCR, expression of GFP-tagged MOT1 in Nicotiana tabacum BY-2 cells under control of the cauliflower mosaic virus 35S RNA promoter near or at the plasma membrane of BY2 cells
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genotyping, expression in protoplast mitochondrial membranes as GFP-tagged protein, quantitative expression analysis by realtime PCR, expression of MOT1 specifically enhances molybdenum accumulation in Saccharomyces cerevisiae by 5fold
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overexpressed in Escherichia coli XL 1-Blue as a C-terminal Strep-tag fusion protein
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activation of modA and modBC genes by TunR in Desulfovibrio vulgaris in vivo
expression of perO is independent of molybdate and sulfate availabilities
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ModC is negatively regulated by the transcription factors MopA and MopB, overview. MopB negatively modulates expression of the mop promoter, and formation of MopA-MopB heteromers, independent of Mo availability, might represent a fine-tuning mechanism controlling mop gene expression. Oligomerization and Mo-binding properties of MopA and MopB, overview
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the periplasmic protein involved in molybdate transport, ModA, is downregulated under high molybdate concentration stress conditions
activation of modA and modBC genes by TunR in Desulfovibrio vulgaris in vivo
activation of modA and modBC genes by TunR in Desulfovibrio vulgaris in vivo
-
-
the periplasmic protein involved in molybdate transport, ModA, is downregulated under high molybdate concentration stress conditions
Oleidesulfovibrio alaskensis
-
the periplasmic protein involved in molybdate transport, ModA, is downregulated under high molybdate concentration stress conditions
Oleidesulfovibrio alaskensis G20
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
specifically binds MoO42-/WO42- but not SO42-, mainly because the desolvation penalty of MoO42-/WO42- is significantly less than that of SO42- and, to a lesser extent, because the large and rigid cavity in these proteins attenuates ligand interactions with SO42-, as compared to MoO42-, exclusion of positively charged Lys/Arg side chains in the anion-binding sites of ModA, because Lys/Arg do not contribute to the selectivity of the binding pocket and substantially stabilize the complex between the oxyanion and protein ligands, which in turn would prohibit the rapid release of the bound oxyanion at a certain stage during the transport process
additional information
-
transcription of modABC genes is repressed by molybdate
additional information
-
transcription of modABC genes is repressed by molybdate
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Grunden, A.M.; Shanmugam, K.T.
Molybdate transport and regulation in bacteria
Arch. Microbiol.
168
345-354
1997
Azotobacter vinelandii, Bradyrhizobium japonicum, Clostridium pasteurianum, Escherichia coli, Haemophilus influenzae, Rhodobacter capsulatus
brenda
Neubauer, H.; Pantel, I.; Lindgren, P.E.; Gtz, F.
Characterization of the molybdate transport system ModABC of Staphylococcus carnosus
Arch. Microbiol.
172
109-115
1999
Staphylococcus carnosus
brenda
Wang, G.; Angermueller, S.; Klipp, W.
Characterization of Rhodobacter capsulatus genes encoding a molybdenum transport system and putative molybdenum-pterin-binding proteins
J. Bacteriol.
175
3031-3042
1993
Rhodobacter capsulatus
brenda
Menendez, C.; Otto, A.; Igloil, G.; Nick, P.; Brandsch, R.; Schubach, B.; Bottcher, B.; Brandsch, R.
Molybdate-uptake genes and molybdopterin-biosynthesis genes on a bacterial plasmid. Characterization of MoeA as a filament-forming protein with adenosinetriphosphatase activity
Eur. J. Biochem.
250
524-531
1997
Paenarthrobacter nicotinovorans
brenda
Self, W.T.; Grunden, A.M.; Hasona, A.; Shanmugam, K.T.
Molybdate transport
Res. Microbiol.
152
311-321
2001
Aeropyrum pernix, Aquifex aeolicus, Azotobacter vinelandii, Bacillus subtilis, Campylobacter jejuni, Deinococcus radiodurans, Escherichia coli, Haemophilus influenzae, Haloferax volcanii, Helicobacter pylori, Methanopyrus kandleri, Methanothermobacter thermautotrophicus, Mycobacterium tuberculosis, Paenarthrobacter nicotinovorans, Pseudomonas aeruginosa, Pyrococcus abyssi, Pyrococcus furiosus, Pyrococcus horikoshii, Rhodobacter capsulatus, Staphylococcus carnosus, Streptomyces coelicolor, Synechocystis sp., Vibrio cholerae serotype O1
brenda
Makdessi, K.; Fritsche, K.; Pich, A.; Andreesen, J.R.
Identification and characterization of the cytoplasmic tungstate/molybdate-binding protein (Mop) from Eubacterium acidaminophilum
Arch. Microbiol.
181
45-51
2004
Peptoclostridium acidaminophilum, Peptoclostridium acidaminophilum DSM 3953
brenda
Dudev, T.; Lim, C.
Oxyanion selectivity in sulfate and molybdate transport proteins: An ab initio/CDM study
J. Am. Chem. Soc.
126
10296-10305
2004
Azotobacter vinelandii
brenda
Delgado, M.J.; Tresierra-Ayala, A.; Talbi, C.; Bedmar, E.J.
Functional characterization of the Bradyrhizobium japonicum modA and modB genes involved in molybdenum transport
Microbiology
152
199-207
2006
Bradyrhizobium japonicum, Bradyrhizobium japonicum USDA 110
brenda
Zahalak, M.; Pratte, B.; Werth, K.J.; Thiel, T.
Molybdate transport and its effect on nitrogen utilization in the cyanobacterium Anabaena variabilis ATCC 29413
Mol. Microbiol.
51
539-549
2004
Trichormus variabilis
brenda
Kashyap, D.R.; Botero, L.M.; Lehr, C.; Hassett, D.J.; McDermott, T.R.
A Na+:H+ antiporter and a molybdate transporter are essential for arsenite oxidation in Agrobacterium tumefaciens
J. Bacteriol.
188
1577-1584
2006
Agrobacterium tumefaciens (Q2L7J6), Agrobacterium tumefaciens
brenda
Tomatsu, H.; Takano, J.; Takahashi, H.; Watanabe-Takahashi, A.; Shibagaki, N.; Fujiwara, T.
An Arabidopsis thaliana high-affinity molybdate transporter required for efficient uptake of molybdate from soil
Proc. Natl. Acad. Sci. USA
104
18807-18812
2007
Arabidopsis thaliana
brenda
Baxter, I.; Muthukumar, B.; Park, H.C.; Buchner, P.; Lahner, B.; Danku, J.; Zhao, K.; Lee, J.; Hawkesford, M.J.; Guerinot, M.L.; Salt, D.E.
Variation in molybdenum content across broadly distributed populations of Arabidopsis thaliana is controlled by a mitochondrial molybdenum transporter (MOT1)
PLoS Genet.
4
e1000004
2008
Arabidopsis thaliana
brenda
Gerber, S.; Comellas-Bigler, M.; Goetz, B.A.; Locher, K.P.
Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter
Science
321
246-250
2008
Methanosarcina acetivorans (Q8TTZ3), Methanosarcina acetivorans
brenda
Wiethaus, J.; Mueller, A.; Neumann, M.; Neumann, S.; Leimkuehler, S.; Narberhaus, F.; Masepohl, B.
Specific interactions between four molybdenum-binding proteins contribute to Mo-dependent gene regulation in Rhodobacter capsulatus
J. Bacteriol.
191
5205-5215
2009
Rhodobacter capsulatus
brenda
Taveirne, M.E.; Sikes, M.L.; Olson, J.W.
Molybdenum and tungsten in Campylobacter jejuni: their physiological role and identification of separate transporters regulated by a single ModE-like protein
Mol. Microbiol.
74
758-771
2009
Campylobacter jejuni
brenda
Chan, S.; Giuroiu, I.; Chernishof, I.; Sawaya, M.R.; Chiang, J.; Gunsalus, R.P.; Arbing, M.A.; Perry, L.J.
Apo and ligand-bound structures of ModA from the archaeon Methanosarcina acetivorans
Acta Crystallogr. Sect. F
66
242-250
2010
Methanosarcina acetivorans
brenda
Aguilar-Barajas, E.; Diaz-Perez, C.; Ramirez-Diaz, M.I.; Riveros-Rosas, H.; Cervantes, C.
Bacterial transport of sulfate, molybdate, and related oxyanions
Biometals
24
687-707
2011
Azotobacter vinelandii, Archaeoglobus fulgidus, Escherichia coli, Pyrococcus horikoshii, Rhodobacter capsulatus, Methanosarcina acetivorans, Xanthomonas axonopodis
brenda
Gisin, J.; Mueller, A.; Pfaender, Y.; Leimkuehler, S.; Narberhaus, F.; Masepohl, B.
A Rhodobacter capsulatus member of a universal permease family imports molybdate and other oxyanions
J. Bacteriol.
192
5943-5952
2010
Rhodobacter capsulatus
brenda
Tirado-Lee, L.; Lee, A.; Rees, D.C.; Pinkett, H.W.
Classification of a Haemophilus influenzae ABC transporter HI1470/71 through its cognate molybdate periplasmic binding protein, MolA
Structure
19
1701-1710
2011
Haemophilus influenzae
brenda
Otrelo-Cardoso, A.R.; Nair, R.R.; Correia, M.A.; Rivas, M.G.; Santos-Silva, T.
TupA: a tungstate binding protein in the periplasm of Desulfovibrio alaskensis G20
Int. J. Mol. Sci.
15
11783-11798
2014
Oleidesulfovibrio alaskensis, Oleidesulfovibrio alaskensis G20
brenda
Kazakov, A.E.; Rajeev, L.; Luning, E.G.; Zane, G.M.; Siddartha, K.; Rodionov, D.A.; Dubchak, I.; Arkin, A.P.; Wall, J.D.; Mukhopadhyay, A.; Novichkov, P.S.
New family of tungstate-responsive transcriptional regulators in sulfate-reducing bacteria
J. Bacteriol.
195
4466-4475
2013
Desulfovibrio vulgaris (Q72FN2), Desulfovibrio vulgaris (Q72FN3), Desulfovibrio vulgaris (Q72FN6), Desulfovibrio vulgaris Hildenborough (Q72FN2), Desulfovibrio vulgaris Hildenborough (Q72FN3), Desulfovibrio vulgaris Hildenborough (Q72FN6)
brenda
Rice, A.J.; Alvarez, F.J.; Schultz, K.M.; Klug, C.S.; Davidson, A.L.; Pinkett, H.W.
EPR spectroscopy of MolB2C2-a reveals mechanism of transport for a bacterial type II molybdate importer
J. Biol. Chem.
288
21228-21235
2013
Haemophilus influenzae
brenda
Rice, A.J.; Harrison, A.; Alvarez, F.J.; Davidson, A.L.; Pinkett, H.W.
Small substrate transport and mechanism of a molybdate ATP binding cassette transporter in a lipid environment
J. Biol. Chem.
289
15005-15013
2014
Haemophilus influenzae (Q57399), Haemophilus influenzae, Haemophilus influenzae RD (Q57399)
brenda
Vigonsky, E.; Ovcharenko, E.; Lewinson, O.
Two molybdate/tungstate ABC transporters that interact very differently with their substrate binding proteins
Proc. Natl. Acad. Sci. USA
110
5440-5445
2013
Archaeoglobus fulgidus, Archaeoglobus fulgidus (O30144), Haemophilus influenzae, Haemophilus influenzae (Q4QJQ0)
brenda
Demtroeder, L.; Narberhaus, F.; Masepohl, B.
Coordinated regulation of nitrogen fixation and molybdate transport by molybdenum
Mol. Microbiol.
111
17-30
2019
Sinorhizobium meliloti
brenda
Cheng, G.; Karunakaran, R.; East, A.K.; Poole, P.S.
Multiplicity of sulfate and molybdate transporters and their role in nitrogen fixation in Rhizobium leguminosarum bv. viciae Rlv3841
Mol. Plant Microbe Interact.
29
143-152
2016
Rhizobium leguminosarum bv. viciae, Rhizobium leguminosarum bv. viciae Rlv3841
brenda
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