Information on EC 3.6.3.25 - sulfate-transporting ATPase

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

EC NUMBER
COMMENTARY hide
3.6.3.25
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RECOMMENDED NAME
GeneOntology No.
sulfate-transporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + sulfate/out = ADP + phosphate + sulfate/in
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Sulfur metabolism
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (sulfate-importing)
ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports sulfate and thiosulfate anions.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain H37Rv, gene Rv1739c
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Manually annotated by BRENDA team
strain H37Rv, gene Rv1739c
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Manually annotated by BRENDA team
strain PCC 7942
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Manually annotated by BRENDA team
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 + sulfate/out
ADP + phosphate + sulfate/in
show the reaction diagram
ATP + H2O + thiosulfate/out
ADP + phosphate + thiosulfate/in
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 + sulfate/out
ADP + phosphate + sulfate/in
show the reaction diagram
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transport of sulfate and thiosulfate
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?
ATP + H2O + thiosulfate/out
ADP + phosphate + thiosulfate/in
show the reaction diagram
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transport of sulfate and thiosulfate
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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Na+-independent sulfate uptake
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
carbonyl cyanide 3-chloro-phenylhydrazone
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N-ethylmaleimide
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additional information
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no inhibition by bicarbonate, nitrate, or phosphate, or by the anion transport inhibitor NS3623
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4
ATP
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wild type enzyme CysA, at 60°C
0.004
sulfate
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pH 6.0, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
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no activity below pH 5.0 and above pH 8.0
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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ATP-binding protein, associated to
Manually annotated by BRENDA team
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sulfate receptor
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Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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x-ray crystallography
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
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periplasmic sulfate receptor
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain JM109
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inducible expression of Rv1739c in an Escherichia coli strain EWP44 lacking CysA does not increase sulfate uptake by intact cells. Expression of Rv1739c in a Mycobacterium bovis BCG strain lacking the ABC sulfate permease subunit CysA cannot complement sulfate auxotrophy. Induction of Rv1739c expression in Escherichia coli increases bacterial uptake of sulfate, but not Cl-, formate, or oxalate. Sulfate uptake is also increased by overexpression of the Rv1739c transmembrane domain, but not of the cytoplasmic C-terminal STAS domain
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S129C/G46C
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mutation in the periplasmic sulfate receptor, dissociation of sulfate from the mutant enzyme is very slow under oxidizing conditions and increases more than 200-fold when reducing agent is added. This effect is attributed to a loss of interdomain structural flexibility in the presence of the disulfide
additional information
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