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Enzyme Nomenclature
Information on EC 3.6.3.25 - sulfate-transporting ATPase
for references in articles please use BRENDA:EC3.6.3.25
Word Map on EC 3.6.3.25
- 3.6.3.25
- chromatin
- proteasome
- vacuolar
- nucleosome
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mtdnas
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chromatin-remodeling
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proteolipids
- v-atpase
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brahma
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apocytochrome
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non-atpase
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v-type
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male-sterile
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brahma-related
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
3.6.3.25
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RECOMMENDED NAME
GeneOntology No.
sulfate-transporting ATPase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + sulfate/out = ADP + phosphate + sulfate/in
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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 + sulfate/out
ADP + phosphate + sulfate/in
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?
ATP + H2O + sulfate/out
ADP + phosphate + sulfate/in
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transport of sulfate and thiosulfate
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?
ATP + H2O + sulfate/out
ADP + phosphate + sulfate/in
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facilitation of bacterial sulfate uptake by Rv1739c requires CysA and its associated sulfate permease activity, thus Rv1739c may be a CysTWA-dependent sulfate transporter
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-
?
ATP + H2O + sulfate/out
ADP + phosphate + sulfate/in
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facilitation of bacterial sulfate uptake by Rv1739c requires CysA and its associated sulfate permease activity, thus Rv1739c may be a CysTWA-dependent sulfate transporter
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?
ATP + H2O + thiosulfate/out
ADP + phosphate + thiosulfate/in
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?
ATP + H2O + thiosulfate/out
ADP + phosphate + thiosulfate/in
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transport of sulfate and thiosulfate
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?
ATP + H2O + thiosulfate/out
ADP + phosphate + thiosulfate/in
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thiosulfate can be transported by two permease systems. One of theses systems is the sulfate permease, while the other does not required cysT and cysW gene products but uses other integral membrane components
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?
additional information
?
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facilitation of bacterial sulfate uptake by Rv1739c requires CysA and its associated sulfate permease activity, thus Rv1739c may be a CysTWA-dependent sulfate transporter
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additional information
?
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facilitation of bacterial sulfate uptake by Rv1739c requires CysA and its associated sulfate permease activity, thus Rv1739c may be a CysTWA-dependent sulfate transporter
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additional information
?
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Na+-independent sulfate uptake
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + sulfate/out
ADP + phosphate + sulfate/in
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transport of sulfate and thiosulfate
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?
ATP + H2O + thiosulfate/out
ADP + phosphate + thiosulfate/in
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transport of sulfate and thiosulfate
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?
additional information
?
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facilitation of bacterial sulfate uptake by Rv1739c requires CysA and its associated sulfate permease activity, thus Rv1739c may be a CysTWA-dependent sulfate transporter
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additional information
?
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facilitation of bacterial sulfate uptake by Rv1739c requires CysA and its associated sulfate permease activity, thus Rv1739c may be a CysTWA-dependent sulfate transporter
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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the ABC-transoprter consists of both the membrane components - the products of the genes cysT, cysW and cysA and the periplasmic binders - the products of the genes cysP and sbp
additional information
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identification of the cysP gene product as a thiosulfate-binding protein
additional information
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cysA encodes the membrane-associated ATP-binding protein, sbpA encodes the sulfate-binding protein, cysT and cysW encode proteins that may form a channel for the transport of sulfate across the cytoplasmic membrane, cysT encodes a polypeptide that has some homology to a family of prokaryotic regulatory proteins
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
additional information
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mutation to serine of the three cysteine residues of Rv1739c does not affect magnitude, pH-dependence, or pharmacology of sulfate uptake
additional information
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mutation to serine of the three cysteine residues of Rv1739c does not affect magnitude, pH-dependence, or pharmacology of sulfate uptake
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