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Enzyme Nomenclature
Information on EC 3.6.3.12 - K+-transporting ATPase
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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EC NUMBER 
COMMENTARY 
3.6.3.12
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RECOMMENDED NAME
GeneOntology No.
K+-transporting ATPase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + K+/out = ADP + phosphate + K+/in
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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-
-
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transmembrane transport
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-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (K+-importing)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A bacterial enzyme of di(heterotetrameric) structure that is involved in K+ import. The probable stoichiometry is one ion per ATP hydrolysed.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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the ATP-hydrolyzing subunit KdpB in the transport complex is classified as type IA P-type ATPase
physiological function
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high-affinity potassium uptake is mediated by the ATP-driven KdpFABC complex. The KdpA subunit promotes K+ transport
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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 + K+/out
ADP + phosphate + K+/in
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inducible, ATP-driven high-affinity K+ uptake system in Halobacterium, overview. Strain R1 adapts to K+ limitation by a significant decrease of the intracellular K+ level, which suggests a rather complex mechanism of K+ homeostasis, in which the adaptation of cellular K+ concentrations and the concomitant transcriptional regulation of genes coding for a high-affinity ATP-driven K+ uptake system ensure the essential potassium supply under limiting conditions. K+ is a growth-limiting factor for Halobacterium salinarum R1
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-
?
ATP + H2O + K+/out
ADP + phosphate + K+/in
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inducible, ATP-driven high-affinity K+ uptake system in Halobacterium, overview. Strain R1 adapts to K+ limitation by a significant decrease of the intracellular K+ level, which suggests a rather complex mechanism of K+ homeostasis, in which the adaptation of cellular K+ concentrations and the concomitant transcriptional regulation of genes coding for a high-affinity ATP-driven K+ uptake system ensure the essential potassium supply under limiting conditions. K+ is a growth-limiting factor for Halobacterium salinarum R1
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-
?
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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 + K+/out
ADP + phosphate + K+/in
-
inducible, ATP-driven high-affinity K+ uptake system in Halobacterium, overview. Strain R1 adapts to K+ limitation by a significant decrease of the intracellular K+ level, which suggests a rather complex mechanism of K+ homeostasis, in which the adaptation of cellular K+ concentrations and the concomitant transcriptional regulation of genes coding for a high-affinity ATP-driven K+ uptake system ensure the essential potassium supply under limiting conditions. K+ is a growth-limiting factor for Halobacterium salinarum R1
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-
?
ATP + H2O + K+/out
ADP + phosphate + K+/in
-
inducible, ATP-driven high-affinity K+ uptake system in Halobacterium, overview. Strain R1 adapts to K+ limitation by a significant decrease of the intracellular K+ level, which suggests a rather complex mechanism of K+ homeostasis, in which the adaptation of cellular K+ concentrations and the concomitant transcriptional regulation of genes coding for a high-affinity ATP-driven K+ uptake system ensure the essential potassium supply under limiting conditions. K+ is a growth-limiting factor for Halobacterium salinarum R1
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Cu2+
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induces the efflux of potassium ions from both cells and spheroplasts
K+
Mg2+
Mn2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-O-3-hydroxyhexanoyl-beta-D-glucopyranosyl(1-4)-(6-O-acetyl-beta-D-glucopyranosyl(1-16)-2,15,16-trihydroxyhexadecanoic acid)
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a natural fungicide, i.e. CL, produced by the yeast Pseudozyma fusiformata VKM Y-2821, induces the efflux of potassium ions from both cells and spheroplasts
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Cat3 protein
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required for enzyme gene cluster expression and activity, encoded by an additional ORF located immediately downstream of the kdpFABC gene cluster, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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ATPase activity and ATP binding affinity of wild-type and mutant enzyme complexes, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
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quantitative analysis of K+-dependent growth and K+-induced kdpFABCcat3 gene expression, overview
additional information
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quantitative analysis of K+-dependent growth and K+-induced kdpFABCcat3 gene expression, overview
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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obtained by treating cells with lyophilized gastric juice of edible snails in 5% citric buffer with 0.8 M mannitol, pH 6.5
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obtained by treating cells with lyophilized gastric juice of edible snails in 5% citric buffer with 0.8 M mannitol, pH 6.5
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21000
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1 * 59000 + 1 * 72000 + 1 * 21000 + 1 * 4000-6000, SDS-PAGE; 1 * 59000 + 1 * 72000 + 1 * 21000, SDS-PAGE
22000
59000
72000
74000
79000
59000
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1 * 59000 + 1 * 72000 + 1 * 21000 + 1 * 4000-6000, SDS-PAGE; 1 * 59000 + 1 * 72000 + 1 * 21000, SDS-PAGE
72000
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1 * 59000 + 1 * 72000 + 1 * 21000 + 1 * 4000-6000, SDS-PAGE; 1 * 59000 + 1 * 72000 + 1 * 21000, SDS-PAGE
72000
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2 * 72000, SDS-PAGE, functional and structural dimeric enzyme with a close vicinity of two KdpB subunits within the functional KdpFABC complex, a dissociation constant for a monomer/dimer equilibrium between 30 and 50 nM, structure, overview
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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2 * 72000, SDS-PAGE, functional and structural dimeric enzyme with a close vicinity of two KdpB subunits within the functional KdpFABC complex, a dissociation constant for a monomer/dimer equilibrium between 30 and 50 nM, structure, overview
tetramer
trimer
tetramer
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1 * 59000 + 1 * 72000 + 1 * 21000 + 1 * 4000-6000, SDS-PAGE
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trimer
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; 1 * 58189 + 1 * 72112 + 1 * 20267, DNA-sequence analysis; 1 * 58189 + 1 * 72112 + 1 * 20267, DNA-sequence analysis; 1 * 79000 + 1 * 74000 + 1 * 22000, SDS-PAGE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzyme complexes from Escherichia coli strain BL21
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning and expression of wild-type and mutant enzyme complexes in Escherichia coli strain BL21
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expressed in Escherichia coli
expression in Escherichia coli
kdpFABC gene cluster, strain R1 comprises one single gene cluster containing the genes kdpFABC coding for homologs of the bacterial ATP-driven K+ uptake system KdpFABC, genes kdpB and kdpC as well as kdpC and cat3 do overlap by one base pair, genetic organization and regulation, overview
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTAkdpX
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truncation of the kdpX gene leads to a less efficient K+-pump than wild-type
DELTAkdpY
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truncation of the kdpY gene has a significant impact on the growth of the Escherichia coli mutant TK2205, which is unable to grow at low potassium concentrations
DELTAkdpZ
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truncation of the kdpZ gene has a significant impact on the growth of the Escherichia coli mutant TK2205, which is unable to grow at low potassium concentrations
Q140A
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site-directed mutagenesis, the mutant is still able to tolerate extreme potassium limitations below 0.1 mM, but shows 38% reduced growth compared to the wild-type
Q140A/R143A/V144A/A145S/A147S/R148A/L150A
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site-directed mutagenesis of the complete 140-QIPRVAKARNL-150 ATP binding motif in KdpC, the mutant cells comprising a complete exchange of the signature motif show no growth if the potassium concentration drops below 5 mM
Q140E
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site-directed mutagenesis, the mutant is still able to tolerate extreme potassium limitations below 0.1 mM, but shows 38% reduced growth compared to the wild-type
Q140N
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site-directed mutagenesis, the mutant is still able to tolerate extreme potassium limitations below 0.1 mM, but shows 12% reduced growth compared to the wild-type
additional information
additional information
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the 140-QIPRVAKARNL-150 ATP binding motif in KdpC is deleted completely, resulting in mutant DELTAQ-L, cells comprising a deletion of the signature motif showed no growth if the potassium concentration drops below 5 mM. The mutations generated result in different phenotypes with respect to tolerance of potassium limitation, overview
additional information
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expression of plasmid-encoded kdpFABCcat3 is sufficient to complement the phenotype of a chromosomal kdpFABCcat3 deletion strain, whereas expression of only kdpFABC is not
additional information
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expression of plasmid-encoded kdpFABCcat3 is sufficient to complement the phenotype of a chromosomal kdpFABCcat3 deletion strain, whereas expression of only kdpFABC is not
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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