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Information on EC 7.2.2.9 - P-type Cu2+ transporter and Organism(s) Archaeoglobus fulgidus and UniProt Accession O30085

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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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Archaeoglobus fulgidus
UNIPROT: O30085
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Word Map
The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
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
adenosine 5'-triphosphatase
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-
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ATP hydrolase
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-
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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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-
-
-
MNK
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-
-
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Pinal night-specific ATPase
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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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-
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Wilson disease-associated protein homolog
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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
ATP + H2O + Cu2+/in
ADP + phosphate + Cu2+/out
show the reaction diagram
-
-
-
?
ATP + H2O + Cu2+in
ADP + phosphate + Cu2+out
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Cu2+/in
ADP + phosphate + Cu2+/out
show the reaction diagram
-
-
-
?
ATP + H2O + Cu2+in
ADP + phosphate + Cu2+out
show the reaction diagram
CopB drives the efflux of Cu2+ from the cell
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ag+
partially activated by Ag+, 55%, of the activation compared to Cu2+
Cu+
partially activated by Cu+, 22% of the activation compared to Cu2+
Cu2+
activated by Cu2+ with high apparent affinity (K1/2 = 0.00028 mM)
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
CopB drives the efflux of Cu2+ from the cell
additional information
-
mutation of the HP-motif and the Gly-rich sequence in the N-domain impairs ATP binding
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization and structure determination of the the apo- and phosphate-bound ATP-binding domain, hanging drop vapour diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
delM1-M54
a truncated CopB lacking the first 54 amino acids is constructed to characterize the N-terminal metal binding domain. This enzyme shows reduced ATPase activity (50% of wild type) but no changes in metal selectivity, ATP dependence, or phosphorylation levels
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant ATP-binding domain
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of the ATP-binding domain in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jayakanthan, S.; Roberts, S.A.; Weichsel, A.; Argello, J.M.;, McEvoy, M.M.
Conformations of the apo-, substrate-bound and phosphate-bound ATP-binding domain of the Cu(II) ATPase CopB illustrate coupling of domain movement to the catalytic cycle
Biosci. Rep.
32
443-453
2012
Archaeoglobus fulgidus (O30085)
Manually annotated by BRENDA team
Mana-Capelli, S.; Mandal, A.K.; Argello, J.M.
Archaeoglobus fulgidus CopB is a thermophilic Cu2+-ATPase: functional role of its histidine-rich-N-terminal metal binding domain
J. Biol. Chem.
278
40534-40541
2003
Archaeoglobus fulgidus (O30085), Archaeoglobus fulgidus
Manually annotated by BRENDA team