Information on EC 3.6.3.55 - tungstate-importing ATPase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
3.6.3.55
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RECOMMENDED NAME
GeneOntology No.
tungstate-importing ATPase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + tungstate[side 1] = ADP + phosphate + tungstate[side 2]
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (tungstsate-importing)
An ABC-type (ATP-binding cassette-type) ATPase. The enzymes from the archaeon Pyrococcus furiosus, the Gram-positive bacterium Eubacterium acidaminophilum and the Gram-negative bacterium Campylobacter jejuni transport tungsten into the cell for incorporation into tungsten-dependent enzymes.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
component TupA; gene Dde_0234 or tupA encoding component TupA, organized in the gene cluster tupABC
UniProt
Manually annotated by BRENDA team
component TupA; gene Dde_0234 or tupA encoding component TupA, organized in the gene cluster tupABC
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
tupA; genes tupABC coding for an ABC transporter specific for tungstate
UniProt
Manually annotated by BRENDA team
tupA; genes tupABC coding for an ABC transporter specific for tungstate
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
show the reaction diagram
ATP + H2O + tungstate[side 1]
ADP + phosphate + tungstate[side 2]
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + tungstate/out
ADP + phosphate + tungstate/in
show the reaction diagram
ATP + H2O + tungstate[side 1]
ADP + phosphate + tungstate[side 2]
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
vanadate
additional information
no impairment of tungstate uptake is observed if the ATPase inhibitor arsenate or the uncoupler 2,4-dinitrophenol are present during the uptake experiments by resting cells
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.69
isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
x * 29000, recombinant enzyme, SDS-PAGE
40000
native PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Cj1540 contains a simpler N-terminal signal sequence with a single signal peptidase I cleavage site
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant component TupA, hanging drop vapor diffusion method, mixing of 0.002 ml of 7.5 mg/ml protein in 5 mM Tris-HCl, pH 7.5, with 0.001 ml of reservoir solution containing 0.2 M magnesium chloride, 0.1 M HEPES, pH 7.5, and 30% w/v PEG 3350, 20°C, 4 days, X-ray diffraction structure determination and analysis at 1.4 A resolution, molecular replacement
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
6 h, no precipiotation is observed
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant soluble component TupA from Escherichia coli strain BL21 (DE3) by anion exchange chromatography, gel filtration, and ultrafiltration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21(DE3)
expression in TOP10 cell
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)
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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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; activation of modA and modBC genes by TunR in Desulfovibrio vulgaris in vivo
genetic regulation of tupA and modA, overview
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the protein involved in tungstate transport (TupA) is downregulated under high molybdate concentration stress conditions
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D160A
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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
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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
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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
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mutant is able to bind both molybdate and tungstate but with lower affinities than wild-type WtpA. Mutant retains specificity for tungstate
additional information
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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