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Information on EC 7.2.2.9 - P-type Cu2+ transporter and Organism(s) Saccharolobus solfataricus and UniProt Accession Q97UU7

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EC Tree
IUBMB Comments
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme from the termophilic archaeon Archaeoglobus fulgidus is involved in copper extrusion from the cell [1,2].
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Saccharolobus solfataricus
UNIPROT: Q97UU7
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The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
atp7b, atp7a, copper transporter, copper-transporting atpase, copper-transporting p-type atpase, menkes protein, cu-atpase, copper transporting p-type atpase, copper atpase, copper-transporting p-type, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper transporting ATPase
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adenosine 5'-triphosphatase
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ATP hydrolase
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ATP phosphohydrolase
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-
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ATP7B
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-
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ATPase
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-
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complex V
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-
-
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Cu2+-ATPase
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-
-
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CUA-1 ATPase
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-
-
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Menkes disease-associated protein
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-
-
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Menkes disease-associated protein homolog
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-
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Menkes P-type ATPase
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-
-
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MNK
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-
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Pinal night-specific ATPase
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-
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WCBD
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-
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Wilson copper-transporting P-type ATPase
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-
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Wilson disease copper-transporting ATPase
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-
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Wilson disease protein
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-
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Wilson disease-associated protein
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Wilson disease-associated protein homolog
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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 (P-type, Cu2+-exporting)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme from the termophilic archaeon Archaeoglobus fulgidus is involved in copper extrusion from the cell [1,2].
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
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study of the mechanism of ATP hydrolysis of a shortened variant of the heavy metal-translocating P-type ATPase CopB. Stoichiometric high-affinity binding of one nucleotide to the protein is demonstrated. The phosphate groups are not involved in nucleotide binding. A model of the hydrolytic mechanism is suggested
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
CopB-B has heavy metal stimulated phosphatase activity, which is half maximal in the presence of 80 microM Cu2+
Mg2+
not necessary for nucleotide association but essential for the phosphatase activity
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
integral membrane protein
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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deletion mutant analysis demonstrates that CopB is low-affinity copper export ATPase. For the DELTAcopB mutant strain 1.4 mM CuSO4 is needed to slow the onset and beginning of stationary phase at lower levels
physiological function
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CopB is low-affinity copper export ATPase. CopA and CopB act as resistance factors to copper ions at overlapping concentrations. CopB is also involved in resistance to silver
malfunction
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deletion mutant analysis demonstrates that CopA is an effective copper pump at low and high copper concentrations. The DELTAcopA mutant shows highly reduced growth at 2 mM. High toxicity of copper to the DELTAcopA
physiological function
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CopA is an effective copper pump at low and high copper concentrations. CopA and CopB act as resistance factors to copper ions at overlapping concentrations. CopA is also involved in resistance to silver
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization trials are performed at 18 °C by vapor diffusion using the hanging-drop technique, crystal structure of the catalytic fragment of a Sulfolobus solfataricus P-type ATPase, CopB-B, is determined with a 2.6 A resolution.In CopB-B crystals, a bound sulfate anion is identified at the phosphate-binding location. In solution state bound phosphate can be readily displaced by orthovanadate at submillimolar concentration as well as by sulfate at millimolar concentration. It is possible to assign the structure of the sulfate-bound phosphorylation domain of CopB-B to a state related to an enzyme/phosphate intermediate state of the catalytic cycle
hangimg drop vapour diffusion method, 3D crystals of CopB-B, the 29 kDa catalytic ATP binding/phosphorylation domain are produced, which diffracted to a resolution of 2.2 A
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of three different soluble domains of the protein (CopB-A), CopB-B (ATP binding/phosphorylation domain), and CopB-C (cation binding domain)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of three different soluble domains of the protein (CopB-A (phosphatase domain), CopB-B, and CopB-C) in Escherichia coli
the catalytic fragment CopB-B is expressed in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
synthesized at low levels under standard growth conditions (i.e. under copper limitation), and the expression levels increases after addition of copper
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synthesized at low levels under standard growth conditions (i.e. under copper limitation), and the expression levels increases after addition of copper
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Völlmecke, C.; Kötting, C.; Gerwert, K.; Lübben, M.
Spectroscopic investigation of the reaction mechanism of CopB-B, the catalytic fragment from an archaeal thermophilic ATP-driven heavy metal transporter
FEBS J.
276
6172-6186
2009
Saccharolobus solfataricus (Q97UU7)
Manually annotated by BRENDA team
Deigweiher, K.; Drell, T.L.; Prutsch, A.; Scheidig, A.J.; Luebben, M.
Expression, isolation, and crystallization of the catalytic domain of CopB, a putative copper transporting ATPase from the thermoacidophilic archaeon Sulfolobus solfataricus
J. Bioenerg. Biomembr.
36
151-159
2004
Saccharolobus solfataricus (Q97UU7), Saccharolobus solfataricus
Manually annotated by BRENDA team
Lübben, M.; Güldenhaupt, J.; Zoltner, M.; Deigweiher, K.; Haebel, P.; Urbanke, C.; Scheidig, A.J.
Sulfate acts as phosphate analog on the monomeric catalytic fragment of the CPx-ATPase CopB from Sulfolobus solfataricus
J. Mol. Biol.
369
368-385
2007
Saccharolobus solfataricus (Q97UU7), Saccharolobus solfataricus
Manually annotated by BRENDA team