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Information on EC 7.3.2.5 - ABC-type molybdate transporter
for references in articles please use BRENDA:EC7.3.2.5
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EC Tree 7 Translocases
7.3 Catalysing the translocation of inorganic anions and their chelates
7.3.2 Linked to the hydrolysis of a nucleoside triphosphate
7.3.2.5 ABC-type molybdate transporter
IUBMB 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.
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, moda/wtpa, wtpabc, molybdenum transporter, molybdate importer, more
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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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-
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molybdate transporter
molybdate- or tungstate-binding protein
molybdate-transporting ATPase
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molybdate/tungstate ABC transporter
MOP
Mot1.2
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
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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
MetaCyc
molybdenum cofactor biosynthesis
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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
LITERATURE
COMMENTARY
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
Substrates: -
Products: -
Products: -
?
ATP + H2O + chromate/out
?
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + molybdate/out
?
-
Substrates: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Substrates: the enzyme is essential for arsenite oxidation
Products: -
Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Substrates: -
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Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: two ATP per imported molybdate
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Substrates: -
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Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: enzyme is involved in molybdate transport
Products: -
Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: import of molybdate
Products: -
Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: sulfate and phosphate are not effective ligands for ModA
Products: -
Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Substrates: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Substrates: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Substrates: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Substrates: the ATPase activity is strictly required
Products: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Substrates: -
Products: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: molybdate-bound MaModA employs octahedral coordination of its substrate
Products: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: import of molybdate
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Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: enzyme is involved in molybdate transport
Products: -
Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
Products: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + tungstate/out
?
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: MOT1 is required for efficient uptake and translocation of molybdate and for normal growth under conditions of limited molybdate supply
Products: -
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?
additional information
?
-
-
Substrates: ModABC can also transport tungstate and sulfate. ModA specifically binds molybdate or tungstate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: ModABC can also transport tungstate
Products: -
Products: -
?
additional information
?
-
-
Substrates: ModA specifically binds molybdate and tungstate
Products: -
Products: -
?
additional information
?
-
-
Substrates: mod is primarily a molybdenum transporter that can also transport tungsten, while tup is a tungsten-specific transporter
Products: -
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?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
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Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
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?
additional information
?
-
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Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: ModABC can also transport tungstate and sulfate. ModA specifically binds molybdate or tungstate, WtpABC transports tungstate and molybdate in Pyrococcus furiosus
Products: -
Products: -
?
additional information
?
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Substrates: 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
Products: -
Products: -
?
additional information
?
-
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Substrates: 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
Products: -
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?
additional information
?
-
-
Substrates: sulfate and phosphate have no effect on Mop mobility
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?
additional information
?
-
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Substrates: sulfate and phosphate have no effect on Mop mobility
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?
additional information
?
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Substrates: WtpABC transports tungstate and molybdate in Pyrococcus furiosus, overview
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?
additional information
?
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Substrates: WtpABC transports tungstate and molybdate in Pyrococcus furiosus
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?
additional information
?
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Substrates: 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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Substrates: PerO mediates uptake of molybdate, sulfate, tungstate, and vanadate
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?
additional information
?
-
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Substrates: 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
Products: -
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?
additional information
?
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Substrates: 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
LITERATURE
COMMENTARY
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]
-
Substrates: -
Products: -
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?
ATP + H2O + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
-
Substrates: -
Products: -
Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Substrates: the enzyme is essential for arsenite oxidation
Products: -
Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
Products: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Substrates: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
Products: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: enzyme is involved in molybdate transport
Products: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: import of molybdate
Products: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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Substrates: -
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ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Substrates: -
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ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Substrates: -
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ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Substrates: -
Products: -
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
Substrates: the ATPase activity is strictly required
Products: -
Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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Substrates: -
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ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
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Substrates: -
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ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: import of molybdate
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?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
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ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: enzyme is involved in molybdate transport
Products: -
Products: -
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: MOT1 is required for efficient uptake and translocation of molybdate and for normal growth under conditions of limited molybdate supply
Products: -
Products: -
?
additional information
?
-
-
Substrates: ModABC can also transport tungstate and sulfate. ModA specifically binds molybdate or tungstate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
Products: -
Products: -
?
additional information
?
-
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Substrates: ModABC can also transport tungstate
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is an ABC importer with substrate specificity for molybdate and tungstate
Products: -
Products: -
?
additional information
?
-
-
Substrates: ModABC can also transport tungstate and sulfate. ModA specifically binds molybdate or tungstate, WtpABC transports tungstate and molybdate in Pyrococcus furiosus
Products: -
Products: -
?
additional information
?
-
-
Substrates: WtpABC transports tungstate and molybdate in Pyrococcus furiosus, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: PerO transports molybdate, sulfate, tungstate, and vanadate in Rhodobacter capsulatus functioning as a general oxyanion transporter
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
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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
-
tungstate
-
nicotine degradation is inhibited markedly by addition of tungstate
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
-
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
Nitratidesulfovibrio vulgaris Hildenborough
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
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
Nitratidesulfovibrio vulgaris Hildenborough
gene modA; harbors genes modABC, no tupABC genes
UniProt
brenda
Nitratidesulfovibrio vulgaris Hildenborough
gene modB; harbors genes modABC, no tupABC genes
UniProt
brenda
Nitratidesulfovibrio vulgaris Hildenborough
gene modC; harbors genes modABC, no tupABC genes
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
highly expressed in the blades of the flag leaf and the second leaf during the grain filling stage
brenda
-
high expression level, expression in the protodermal cells behind the root tip, and in epidermis and cortex at the elongation zone
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
MOT1 contains an N-terminal mitochondrial targeting sequence
brenda
-
ModB and ModC, ModB possesses six transmembrane domains
brenda
-
ModB and ModC, ModB possesses six transmembrane domains
brenda
transmembrane domain structure, overview
brenda
-
ModB is a integral membrane, channel-forming protein
brenda
-
ModB is a integral membrane, channel-forming protein
brenda
-
ModB and ModC, ModB possesses six transmembrane domains
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
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
evolution
-
ModABC belongs to the family of molybdate uptake transporters MolT, PerO belongs to the ArsB/NhaD ion transporter family
evolution
-
ModABC belongs to the family of molybdate uptake transporters MolT
evolution
-
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
evolution
-
ModABC belongs to the family of molybdate uptake transporters MolT
evolution
-
ModABC belongs to the family of ATP-binding cassette (ABC) transporters, while PerO is a member of the ArsB/NhaD family
malfunction
-
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
-
metabolism
-
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
Nitratidesulfovibrio vulgaris Hildenborough
-
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
-
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
-
periplasmic binding protein MolA delivers substrate to the ABC transporter MolB2C2
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
-
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
-
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 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
-
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
-
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
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
afModBCA is a high-affinity transport system for molybdate and tungstate anions
physiological function
-
the enzyme is able to scavenge molybdate from the growth medium
physiological function
-
a loss-of-function mutant shows reduced growth compared with wild-type plants when nitrogen fixation is required, but not when nitrogen is provided as nitrate. No effect on molybdenum-dependent nitrate reductase activity is observed, bute nitrogenase activity is severely affected. When grown in the presence of molybdate, yeast expressing MOT1.2 is able to accumulate Mo, with a Vmax of 155 pmol per million cells and h and a k1/2 of 488 nM
physiological function
-
deletion of the ModABC genes abolishes the nicotine-degrading ability. Molybdate at 100 mM fully restores nicotine-degrading activity and recovers growth of the ModABC mutant in a nicotine minimal medium
physiological function
a subunit ModA-disrupted mutant has lost the ability to oxidize substrates in a large extent
physiological function
-
knockout of MOT1:2 leads to more Mo accumulation in roots and less Mo translocation to shoots at the seedling stage and to grains at the maturity stage. The remobilization of Mo from older leaves to young leaves under molybdate-depleted condition is also decreased. Overexpression of MOT1:2 enhances the translocation of Mo from roots to shoots at the seedling stage. Yeast cells expressing Mot1:2 show increased import of Mo
physiological function
Nitratidesulfovibrio vulgaris Hildenborough
-
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
-
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
-
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MODC_HAEIN
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
351
0
39582
Swiss-Prot
-
MODC_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
369
0
38610
Swiss-Prot
other Location (Reliability: 3)
MODC_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
369
0
38610
Swiss-Prot
-
MODC_GRABC
Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1)
367
0
39013
Swiss-Prot
-
MODC_ECOL5
Escherichia coli O6:K15:H31 (strain 536 / UPEC)
352
0
39071
Swiss-Prot
-
MODC_ALCBS
Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2)
358
0
38602
Swiss-Prot
other Location (Reliability: 4)
MODC_RHOPS
Rhodopseudomonas palustris (strain BisB5)
376
0
40008
Swiss-Prot
-
MODC_YERPN
Yersinia pestis bv. Antiqua (strain Nepal516)
359
0
39693
Swiss-Prot
-
MODC_YERPA
Yersinia pestis bv. Antiqua (strain Antiqua)
359
0
39693
Swiss-Prot
-
MODC_RHIJ3
Rhizobium johnstonii (strain DSM 114642 / LMG 32736 / 3841)
355
0
38678
Swiss-Prot
-
MODC_ECOUT
Escherichia coli (strain UTI89 / UPEC)
352
0
39071
Swiss-Prot
-
MODC_SACD2
Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024)
362
0
39082
Swiss-Prot
-
MODC_RHOPB
Rhodopseudomonas palustris (strain BisB18)
381
0
40798
Swiss-Prot
-
MODC_ALBFT
Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
369
0
39702
Swiss-Prot
-
MODC_RHOP2
Rhodopseudomonas palustris (strain HaA2)
377
0
40103
Swiss-Prot
-
MODC_RHIEC
Rhizobium etli (strain ATCC 51251 / DSM 11541 / JCM 21823 / NBRC 15573 / CFN 42)
355
0
38324
Swiss-Prot
-
MODC_HAHCH
Hahella chejuensis (strain KCTC 2396)
358
0
39769
Swiss-Prot
other Location (Reliability: 3)
MODC_BRUA2
Brucella abortus (strain 2308)
359
0
38881
Swiss-Prot
other Location (Reliability: 4)
MODC_RHORT
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1)
370
0
39673
Swiss-Prot
-
MODC_PARM1
Paramagnetospirillum magneticum (strain ATCC 700264 / AMB-1)
363
0
38896
Swiss-Prot
-
MODC_SHIDS
Shigella dysenteriae serotype 1 (strain Sd197)
352
0
39114
Swiss-Prot
-
MODC_SHIBS
Shigella boydii serotype 4 (strain Sb227)
352
0
39086
Swiss-Prot
-
MODC_THIDA
Thiobacillus denitrificans (strain ATCC 25259 / T1)
362
0
39244
Swiss-Prot
-
MODC_PSEPF
Pseudomonas fluorescens (strain Pf0-1)
359
0
39340
Swiss-Prot
-
MODC_DECAR
Dechloromonas aromatica (strain RCB)
359
0
39044
Swiss-Prot
-
MODC_PSE14
Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
362
0
39796
Swiss-Prot
-
MODC_HAEI8
Haemophilus influenzae (strain 86-028NP)
351
0
39520
Swiss-Prot
-
MODC_PSEF5
Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
360
0
39657
Swiss-Prot
-
MODC_PSEU2
Pseudomonas syringae pv. syringae (strain B728a)
362
0
40019
Swiss-Prot
-
MOLC_HAEIN
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
253
0
28520
Swiss-Prot
-
MODC_BRUAB
Brucella abortus biovar 1 (strain 9-941)
359
0
38881
Swiss-Prot
other Location (Reliability: 1)
MODC_ALIF1
Aliivibrio fischeri (strain ATCC 700601 / ES114)
364
0
40271
Swiss-Prot
Secretory Pathway (Reliability: 1)
MODC_SALCH
Salmonella choleraesuis (strain SC-B67)
352
0
39055
Swiss-Prot
-
MODC_SALPA
Salmonella paratyphi A (strain ATCC 9150 / SARB42)
352
0
39055
Swiss-Prot
-
MODC_AROAE
Aromatoleum aromaticum (strain DSM 19018 / LMG 30748 / EbN1)
377
0
40796
Swiss-Prot
-
MODC_METCA
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
356
0
39508
Swiss-Prot
-
MODC_YERPS
Yersinia pseudotuberculosis serotype I (strain IP32953)
359
0
39635
Swiss-Prot
Mitochondrion (Reliability: 2)
MODC_MANSM
Mannheimia succiniciproducens (strain KCTC 0769BP / MBEL55E)
352
0
39307
Swiss-Prot
-
MODC_PECAS
Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)
352
0
39207
Swiss-Prot
other Location (Reliability: 2)
MODC_RHOPA
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
373
0
40000
Swiss-Prot
-
MODC_PHOPR
Photobacterium profundum (strain SS9)
358
0
40497
Swiss-Prot
-
MODC_PHOLL
Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)
354
0
39878
Swiss-Prot
-
MODC_BORPA
Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
369
0
39988
Swiss-Prot
-
MODC_HAEDU
Haemophilus ducreyi (strain 35000HP / ATCC 700724)
351
0
39474
Swiss-Prot
-
MODC_BORPE
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
369
0
40060
Swiss-Prot
-
MODC_BORBR
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
369
0
39988
Swiss-Prot
-
MODC2_BRADU
Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)
897
0
96174
Swiss-Prot
-
MODC1_BRADU
Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)
369
0
39965
Swiss-Prot
-
MODC_PSESM
Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
362
0
39908
Swiss-Prot
-
MODC_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
363
0
38980
Swiss-Prot
other Location (Reliability: 5)
MODC_VIBPA
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
368
0
40933
Swiss-Prot
other Location (Reliability: 1)
MODC_ECOL6
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
352
0
39085
Swiss-Prot
-
MODC_BRUSU
Brucella suis biovar 1 (strain 1330)
359
0
38859
Swiss-Prot
Chloroplast (Reliability: 2)
MODC_SHEON
Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1)
361
0
40552
Swiss-Prot
-
MODC_AGRFC
Agrobacterium fabrum (strain C58 / ATCC 33970)
358
0
39285
Swiss-Prot
-
MODC_BRUME
Brucella melitensis biotype 1 (strain ATCC 23456 / CCUG 17765 / NCTC 10094 / 16M)
359
0
38912
Swiss-Prot
-
MODC_SALTY
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
352
0
39055
Swiss-Prot
other Location (Reliability: 3)
MODC_RHIME
Rhizobium meliloti (strain 1021)
357
0
38720
Swiss-Prot
Chloroplast (Reliability: 2)
MODC_RHILO
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
370
0
39518
Swiss-Prot
-
MODC_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
361
0
39796
Swiss-Prot
-
MODC_VIBCH
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
366
0
40664
Swiss-Prot
other Location (Reliability: 2)
WTPC_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
240
0
27027
Swiss-Prot
-
Q72FN2_NITV2
Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough)
233
0
24741
TrEMBL
-
Q72FN3_NITV2
Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough)
253
0
27978
TrEMBL
-
Q72FN6_NITV2
Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough)
269
0
28201
TrEMBL
-
Q88G97_PSEPK
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
252
0
27044
TrEMBL
-
Q8TTZ3_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
348
0
38851
TrEMBL
other Location (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homohexamer
monomer
additional information
?
-
x * 26700, subunit Moda, x * 24200, subunit ModB, x * 39400, subunit ModC, calculated from sequence
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
-
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
-
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
-
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
-
archaeal ModA proteins possess octahedral coordination, structure of the ModABC complex, overview
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
-
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
-
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
-
ModA 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
-
MolA bound to tungstate and molybdate, X-ray diffraction structure determination and analysis at 1.6 A resolution
-
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
-
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
-
ModA/WtpA molybdate- or tungstate-binding protein crystal structure, conformation of ModA is ellipsoidal and binding of molybdate is through seven hydrogen bonds
-
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
-
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
-
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
-
additional information
-
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
-
additional information
-
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)
-
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
-
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
-
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
-
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
-
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
Nitratidesulfovibrio vulgaris Hildenborough
-
-
the periplasmic protein involved in molybdate transport, ModA, is downregulated under high molybdate concentration stress conditions
-
the periplasmic protein involved in molybdate transport, ModA, is downregulated under high molybdate concentration stress conditions
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
in a whole cell biosynthesis system displaying selective oxidation of furfural to furoic acid, the furancarboxylic acids synthesis is repressed markedly by destroying molybdate transporter
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
Escherichia coli, Clostridium pasteurianum, Bradyrhizobium japonicum, Haemophilus influenzae, Azotobacter vinelandii, 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
Bacillus subtilis, Synechocystis sp., Pseudomonas aeruginosa, Helicobacter pylori, Paenarthrobacter nicotinovorans, Deinococcus radiodurans, Campylobacter jejuni, Mycobacterium tuberculosis, Aquifex aeolicus, Aeropyrum pernix, Escherichia coli, Methanopyrus kandleri, Streptomyces coelicolor, Pyrococcus abyssi, Pyrococcus furiosus, Pyrococcus horikoshii, Staphylococcus carnosus, Haloferax volcanii, Methanothermobacter thermautotrophicus, Azotobacter vinelandii, Rhodobacter capsulatus, Haemophilus influenzae, 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
Escherichia coli, Methanosarcina acetivorans, Rhodobacter capsulatus, Xanthomonas axonopodis, Archaeoglobus fulgidus, Pyrococcus horikoshii, Azotobacter vinelandii
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
Nitratidesulfovibrio vulgaris (Q72FN3), Nitratidesulfovibrio vulgaris (Q72FN2), Nitratidesulfovibrio vulgaris (Q72FN6), Nitratidesulfovibrio vulgaris Hildenborough (Q72FN3), Nitratidesulfovibrio vulgaris Hildenborough (Q72FN2), Nitratidesulfovibrio 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
Zheng, Z.; Xu, Q.; Tan, H.; Zhou, F.; Ouyang, J.
Selective biosynthesis of furoic acid from furfural by Pseudomonas putida and identification of molybdate transporter involvement in furfural oxidation
Front. Chem.
8
587456
2020
Pseudomonas putida (Q88G97)
brenda
Xia, Z.; Lei, L.; Zhang, H.; Wei, H.
Characterization of the ModABC molybdate transport system of Pseudomonas putida in nicotine degradation
Front. Microbiol.
9
3030
2018
Pseudomonas putida
brenda
Hu, D.; Li, M.; Zhao, F.; Huang, X.
The vacuolar molybdate transporter MOT1;2 controls molybdenum remobilization in rice
Front. Plant Sci.
13
863816
2022
Oryza sativa Japonica Group
brenda
Gil-Dixadez, P.; Tejada-Jimenez, M.; Leon-Mediavilla, J.; Wen, J.; Mysore, K.; Imperial, J.; Gonzalez-Guerrero, M.
MtMOT1.2 is responsible for molybdate supply to Medicago truncatula nodules
Plant Cell Environ.
42
310-320
2019
Medicago truncatula
brenda
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