7.3.2.5: ABC-type molybdate transporter
This is an abbreviated version!
For detailed information about ABC-type molybdate transporter, go to the full flat file.
Word Map on EC 7.3.2.5
Reaction
Synonyms
afModBCA, EC 3.6.3.29, HI1470/71, high-affinity molybdate transporter, hiMolBCA, low affinity molybdate transporter, mitochondrial molybdenum transporter, ModA, ModA/WtpA, ModABC, ModABC transporter, ModB, ModBC, ModBCA, ModC, MolA, MolB2C2, MolB2C2-A, MolBC-A, MolBCA, molybdate importer, molybdate transport system, molybdate transporter, molybdate transporter ATPase, molybdate- or tungstate-binding protein, molybdate-transporting ATPase, molybdate/tungstate ABC transporter, molybdenum tansporter 1, molybdenum transporter, MOP, More, MOT1, oxyanion permease, PerO, tungstate/molybdate-binding protein, type II molybdate importer, WtpABC
ECTree
7.3.2.5 ABC-type molybdate transporterAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 7.3.2.5 - ABC-type molybdate transporter
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
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
-
-
-
?
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]
-
-
-
-
?
ATP + H2O + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
-
-
-
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
-
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
the enzyme is essential for arsenite oxidation
-
-
?
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
-
two ATP per imported 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
-
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
-
sulfate and phosphate are not effective ligands for ModA
-
-
?
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
-
-
-
-
?
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
-
molybdate-bound MaModA employs octahedral coordination of its substrate
-
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
-
-
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
-
-
-
?
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
-
-
-
-
?
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
-
enzyme is involved in molybdate transport
-
?
ATP + H2O + molybdate/out
ADP + phosphate + molybdate/in
-
-
-
-
?
additional information
?
-
-
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
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
ModABC can also transport tungstate
-
-
?
additional information
?
-
-
ModA specifically binds molybdate and tungstate
-
-
?
additional information
?
-
-
mod is primarily a molybdenum transporter that can also transport tungsten, while tup is a tungsten-specific 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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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
?
-
Oleidesulfovibrio alaskensis
-
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
-
-
?
additional information
?
-
Oleidesulfovibrio alaskensis G20
-
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
-
-
?
additional information
?
-
-
sulfate and phosphate have no effect on Mop mobility
-
-
?
additional information
?
-
-
sulfate and phosphate have no effect on Mop mobility
-
-
?
additional information
?
-
-
WtpABC transports tungstate and molybdate in Pyrococcus furiosus, overview
-
-
?
additional information
?
-
-
WtpABC transports tungstate and molybdate in Pyrococcus furiosus
-
-
?
additional information
?
-
-
PerO transports molybdate, sulfate, tungstate, and vanadate in Rhodobacter capsulatus functioning as a general oxyanion transporter
-
-
?
additional information
?
-
-
PerO mediates uptake of molybdate, sulfate, tungstate, and vanadate
-
-
?
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
?
-
-
ModA specifically binds Kd of 290 nM for molybdate and 580 nM for tungstate
-
-
?
