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ATP + H2O + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
ATP + H2O + tungstate-[tungstate-binding protein][side 1]
ADP + phosphate + tungstate[side 2] + [tungstate-binding protein][side 1]
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
ATP + H2O + tungstate[side 1]
ADP + phosphate + tungstate[side 2]
additional information
?
-
ATP + H2O + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
Oleidesulfovibrio alaskensis
-
-
-
?
ATP + H2O + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
Oleidesulfovibrio alaskensis G20
-
-
-
?
ATP + H2O + tungstate-[tungstate-binding protein][side 1]
ADP + phosphate + tungstate[side 2] + [tungstate-binding protein][side 1]
-
-
-
-
?
ATP + H2O + tungstate-[tungstate-binding protein][side 1]
ADP + phosphate + tungstate[side 2] + [tungstate-binding protein][side 1]
Oleidesulfovibrio alaskensis
-
-
-
?
ATP + H2O + tungstate-[tungstate-binding protein][side 1]
ADP + phosphate + tungstate[side 2] + [tungstate-binding protein][side 1]
Oleidesulfovibrio alaskensis G20
-
-
-
?
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
-
-
-
-
?
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
the enzyme is part of the the Cj1538-1540 system
-
-
?
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
tungstate binds 50000fold more tightly than molybdate to Cj1540
-
-
?
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
-
-
-
?
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
only tungstate induces a shift of TupA mobility, suggesting that only this anion is specifically bound by TupA. The TupABC transporter is specific for tungstate
-
-
?
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
-
-
-
?
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
only tungstate induces a shift of TupA mobility, suggesting that only this anion is specifically bound by TupA. The TupABC transporter is specific for tungstate
-
-
?
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
the very high affinity WtpABC transporter explains the ability of Pyrococcus furiosus cells to scavenge traces of tungstate from growth medium
-
-
?
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
although reversible binding of molybdate or tungstate by the soluble component WtpA of the archaeal WtpABC transporter enforces a quasi-octahedral coordination onto the molybdenum or tungsten, this does not induce any redox chemistry of the +VI state
-
-
?
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
when the protein is incubated with a mixture of tungstate and molybdate, the amount of bound tungstate is significantly higher, even in the presence of an excess of molybdate during the incubation. WtpA is able to bind tungstate and molybdate, with a preference for tungstate, without changing the oligomeric state of the protein
-
-
?
ATP + H2O + tungstate[side 1]
ADP + phosphate + tungstate[side 2]
-
-
-
-
?
ATP + H2O + tungstate[side 1]
ADP + phosphate + tungstate[side 2]
-
-
-
-
?
ATP + H2O + tungstate[side 1]
ADP + phosphate + tungstate[side 2]
Oleidesulfovibrio alaskensis
-
-
-
?
ATP + H2O + tungstate[side 1]
ADP + phosphate + tungstate[side 2]
Oleidesulfovibrio alaskensis G20
-
-
-
?
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
?
-
-
mod , EC 3.6.3.29, is primarily a molybdenum transporter that can also transport tungsten, while tup is a tungsten-specific transporter
-
-
?
additional information
?
-
-
ModA is able to bind both tungstate and molybdate with very high affinities but is unable to replace one oxoanion with the other in a displacement titration
-
-
?
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
?
-
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
no activity with SO42-, PO43- and ClO4-
-
-
?
additional information
?
-
Oleidesulfovibrio alaskensis G20
no activity with SO42-, PO43- and ClO4-
-
-
?
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
?
-
tungstate uptake by Eubacterium acidaminophilum is not affected by equimolar amounts of molybdate
-
-
?
additional information
?
-
-
tungstate uptake by Eubacterium acidaminophilum is not affected by equimolar amounts of molybdate
-
-
?
additional information
?
-
tungstate uptake by Eubacterium acidaminophilum is not affected by equimolar amounts of molybdate
-
-
?
additional information
?
-
-
the octahedral W(VI)/Mo(VI)-binding motif present in WtpA proteins is essential for its displayed binding preference for tungstate over molybdate
-
-
?
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ATP + H2O + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
ATP + H2O + tungstate-[tungstate-binding protein][side 1]
ADP + phosphate + tungstate[side 2] + [tungstate-binding protein][side 1]
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
ATP + H2O + tungstate[side 1]
ADP + phosphate + tungstate[side 2]
additional information
?
-
ATP + H2O + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
Oleidesulfovibrio alaskensis
-
-
-
?
ATP + H2O + molybdate-[molybdate-binding protein][side 1]
ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
Oleidesulfovibrio alaskensis G20
-
-
-
?
ATP + H2O + tungstate-[tungstate-binding protein][side 1]
ADP + phosphate + tungstate[side 2] + [tungstate-binding protein][side 1]
-
-
-
-
?
ATP + H2O + tungstate-[tungstate-binding protein][side 1]
ADP + phosphate + tungstate[side 2] + [tungstate-binding protein][side 1]
Oleidesulfovibrio alaskensis
-
-
-
?
ATP + H2O + tungstate-[tungstate-binding protein][side 1]
ADP + phosphate + tungstate[side 2] + [tungstate-binding protein][side 1]
Oleidesulfovibrio alaskensis G20
-
-
-
?
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
-
-
-
-
?
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
the enzyme is part of the the Cj1538-1540 system
-
-
?
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
-
-
-
?
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
-
-
-
?
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
the very high affinity WtpABC transporter explains the ability of Pyrococcus furiosus cells to scavenge traces of tungstate from growth medium
-
-
?
ATP + H2O + tungstate[side 1]
ADP + phosphate + tungstate[side 2]
-
-
-
-
?
ATP + H2O + tungstate[side 1]
ADP + phosphate + tungstate[side 2]
-
-
-
-
?
ATP + H2O + tungstate[side 1]
ADP + phosphate + tungstate[side 2]
Oleidesulfovibrio alaskensis
-
-
-
?
ATP + H2O + tungstate[side 1]
ADP + phosphate + tungstate[side 2]
Oleidesulfovibrio alaskensis G20
-
-
-
?
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
?
-
tungstate uptake by Eubacterium acidaminophilum is not affected by equimolar amounts of molybdate
-
-
?
additional information
?
-
-
tungstate uptake by Eubacterium acidaminophilum is not affected by equimolar amounts of molybdate
-
-
?
additional information
?
-
tungstate uptake by Eubacterium acidaminophilum is not affected by equimolar amounts of molybdate
-
-
?
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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, EC 3.6.3.29, 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
tupABC gene encoded enzymes participate in the biosynthesis of the pterin cofactor that is present in molybdenum- and tungsten-containing enzymes except nitrogenase
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
-
tupABC gene encoded enzymes participate in the biosynthesis of the pterin cofactor that is present in molybdenum- and tungsten-containing enzymes except nitrogenase
-
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
-
physiological function
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
physiological function
-
the enzyme provides tungsten for incorporation into the format dehydrogenase, formate dehydrogenase is active in the presence of either tungsten or molybdenum
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
the TupABC system is involved in the cellular uptake of tungsten and belongs to the ABC (ATP binding cassette)-type transporter systems. The TupA component is a periplasmic protein that binds tungstate anions, which are then transported through the membrane by the TupB component using ATP hydrolysis as the energy source, the reaction is catalyzed by the TupC component. The genes encoding the three components are organized in an operon wtpABC or gene cluster (tupABC) regulated by a transcription factor. Under oxoanion starvation, the component A binds tungstate and interacts with the component B to actively transport tungstate from the periplasm to the cytoplasm. The TupABC transport system and, more specifically, the component A may constitute the first selection gate from which cells differentiate between Mo and W. TupA is a tungstate-binding protein that is able to bind tungstate and molybdate ions. Regulation of the transport enzyme complex, overview
physiological function
Oleidesulfovibrio alaskensis G20
-
the TupABC system is involved in the cellular uptake of tungsten and belongs to the ABC (ATP binding cassette)-type transporter systems. The TupA component is a periplasmic protein that binds tungstate anions, which are then transported through the membrane by the TupB component using ATP hydrolysis as the energy source, the reaction is catalyzed by the TupC component. The genes encoding the three components are organized in an operon wtpABC or gene cluster (tupABC) regulated by a transcription factor. Under oxoanion starvation, the component A binds tungstate and interacts with the component B to actively transport tungstate from the periplasm to the cytoplasm. The TupABC transport system and, more specifically, the component A may constitute the first selection gate from which cells differentiate between Mo and W. TupA is a tungstate-binding protein that is able to bind tungstate and molybdate ions. 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
-
additional information
cj1540 (tupA) mutant shows a low cellular tungsten content, and a decrase in formate dehydrogenase activity by about 50% in the tupA strain. Supplementation of the growth medium with tungstate significantly increases formate dehydrogenase activity in the wild-type, while inhibiting known molybdoenzymes
additional information
-
cj1540 (tupA) mutant shows a low cellular tungsten content, and a decrase in formate dehydrogenase activity by about 50% in the tupA strain. Supplementation of the growth medium with tungstate significantly increases formate dehydrogenase activity in the wild-type, while inhibiting known molybdoenzymes
additional information
-
three-dimensional structure modeling
additional information
-
three-dimensional structure modeling
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R118E
Oleidesulfovibrio alaskensis
the mutation prevents the binding of the enzyme to both molybdate and tungstate
R118K
Oleidesulfovibrio alaskensis
the mutant loses the ability to coordinate molybdate and keeps an extremely high affinity and selectivity for tungstate
R118Q
Oleidesulfovibrio alaskensis
the mutant loses the ability to coordinate molybdate and binds tungstate with much less affinity than the wild type enzyme
R118E
Oleidesulfovibrio alaskensis G20
-
the mutation prevents the binding of the enzyme to both molybdate and tungstate
-
R118K
Oleidesulfovibrio alaskensis G20
-
the mutant loses the ability to coordinate molybdate and keeps an extremely high affinity and selectivity for tungstate
-
R118Q
Oleidesulfovibrio alaskensis G20
-
the mutant loses the ability to coordinate molybdate and binds tungstate with much less affinity than the wild type enzyme
-
D160A
-
mutant is able to bind both molybdate and tungstate but with lower affinities than wild-type WtpA. Mutant is no longer able to selectively bind tungstate
D160N
-
mutant is able to bind both molybdate and tungstate but with lower affinities than wild-type WtpA. Mutant is no longer able to selectively bind tungstate
E218A
-
mutant is able to bind both molybdate and tungstate but with lower affinities than wild-type WtpA. Mutant retains specificity for tungstate and displays presence of two binding sites with different affinities
E218Q
-
mutant is able to bind both molybdate and tungstate but with lower affinities than wild-type WtpA. Mutant retains specificity for tungstate
additional information
-
construction of tupB and modA/tupB defective mutants. Supplementation with Na2MoO4 decreases formate dehydrogenase activity in tmutant upB:KAN to 37% of wild-type level, suggesting a preference of tungsten over molybdenum by Tup. 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
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expressed in Escherichia coli Tuner (DE3) cells
Oleidesulfovibrio alaskensis
expression in Escherichia coli BL21(DE3)
gene cj1540 or tupA, overexpression in Campylobacter jejuni strain NCTC 11168, overexpression with TupA native N-terminal signal sequence results in only the mature periplasmic form accumulates, which is highly soluble and stable
gene tupA, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of the soluble TupA component in Escherichia coli strain BL21(DE3)
Oleidesulfovibrio alaskensis
genes tupABC, DNA and amino acid sequence determination and analysis, genetic organization and transcriptional analysis of the sequenced tup genes and the downstream region, phylogenetic analysis and tree, overexpression of the substrate-binding protein of the transporter, TupA, in Escherichia coli
tupA and tupB are two genes in the tungsten transport locus which are divergently transcribed, genetic regulation of tupA/tupB and modA, overview
-
expression in TOP10 cell
-
expression in TOP10 cell
-
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Bevers, L.E.; Hagedoorn, P.; Krijger, G.C.; Hagen, W.R.
Tungsten transport protein A (WtpA) in Pyrococcus furiosus: the first member of a new class of tungstate and molybdate transporters
J. Bacteriol.
188
6498-6505
2006
Pyrococcus furiosus (Q8U4K5)
brenda
Makdessi, K.; Andreesen, J.R.; Pich, A.
Tungstate uptake by a highly specific ABC transporter in Eubacterium acidaminophilum
J. Biol. Chem.
276
24557-24564
2001
Peptoclostridium acidaminophilum (Q93KD6), Peptoclostridium acidaminophilum, Peptoclostridium acidaminophilum DSM 5388 (Q93KD6)
brenda
Smart, J.P.; Cliff, M.J.; Kelly, D.J.
A role for tungsten in the biology of Campylobacter jejuni: tungstate stimulates formate dehydrogenase activity and is transported via an ultra-high affinity ABC system distinct from the molybdate transporter
Mol. Microbiol.
74
742-757
2009
Campylobacter jejuni (Q0P885), Campylobacter jejuni
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
Bevers, L.E.; Schwarz, G.; Hagen, W.R.
A molecular basis for tungstate selectivity in prokaryotic ABC transport systems
J. Bacteriol.
193
4999-5001
2011
Escherichia coli, Pyrococcus furiosus
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 (Q316W1), Oleidesulfovibrio alaskensis G20 (Q316W1)
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
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, Haemophilus influenzae
brenda
Rajeev, L.; Garber, M.E.; Zane, G.M.; Price, M.N.; Dubchak, I.; Wall, J.D.; Novichkov, P.S.; Mukhopadhyay, A.; Kazakov, A.E.
A new family of transcriptional regulators of tungstoenzymes and molybdate/tungstate transport
Environ. Microbiol.
21
784-799
2019
Desulfovibrio vulgaris
brenda
Otrelo-Cardoso, A.R.; Nair, R.R.; Correia, M.A.S.; Cordeiro, R.S.C.; Panjkovich, A.; Svergun, D.I.; Santos-Silva, T.; Rivas, M.G.
Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20
Sci. Rep.
7
5798
2017
Oleidesulfovibrio alaskensis (Q316W1), Oleidesulfovibrio alaskensis G20 (Q316W1)
brenda