Literature summary extracted from
Mana-Capelli, S.; Mandal, A.K.; Argüello, J.M.
Archaeoglobus fulgidus CopB is a thermophilic Cu2+-ATPase: functional role of its histidine-rich-N-terminal metal binding domain (2003), J. Biol. Chem., 278, 40534-40541.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
7.2.2.9 |
expression in Escherichia coli |
Archaeoglobus fulgidus |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
7.2.2.9 |
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 |
Archaeoglobus fulgidus |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
7.2.2.9 |
Ag+ |
partially activated by Ag+, 55%, of the activation compared to Cu2+ |
Archaeoglobus fulgidus |
|
7.2.2.9 |
Cu+ |
partially activated by Cu+, 22% of the activation compared to Cu2+ |
Archaeoglobus fulgidus |
|
7.2.2.9 |
Cu2+ |
activated by Cu2+ with high apparent affinity (K1/2 = 0.00028 mM) |
Archaeoglobus fulgidus |
|
7.2.2.9 |
additional information |
CopB and its homologs are distinguished by a metal binding sequence Cys-Pro-His in their sixth transmembrane segment and a His-rich N-terminal metal binding domain |
Archaeoglobus fulgidus |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
7.2.2.9 |
ATP + H2O + Cu2+in |
Archaeoglobus fulgidus |
CopB drives the efflux of Cu2+ from the cell |
ADP + phosphate + Cu2+out |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
7.2.2.9 |
Archaeoglobus fulgidus |
O30085 |
- |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
7.2.2.9 |
ATP + H2O + Cu2+in |
CopB drives the efflux of Cu2+ from the cell |
Archaeoglobus fulgidus |
ADP + phosphate + Cu2+out |
- |
? |
|
7.2.2.9 |
ATP + H2O + Cu2+in |
the presence of the His residue in the putative transmembrane metal binding site of CopB determines a selectivity for this enzyme that is different for that observed in Cu+/Ag+-ATPases carrying a Cys-Pro-Cys sequence |
Archaeoglobus fulgidus |
ADP + phosphate + Cu2+out |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
7.2.2.9 |
CopB |
the enzyme is a member of the P1B-3-subgroup with a Cys-Pro-His sequence in H6 and 17 His residues within the first 51 amino acids |
Archaeoglobus fulgidus |
7.2.2.9 |
Cu2+-ATPase |
- |
Archaeoglobus fulgidus |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
7.2.2.9 |
55 |
- |
assay at |
Archaeoglobus fulgidus |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
7.2.2.9 |
physiological function |
CopB drives the efflux of Cu2+ from the cell |
Archaeoglobus fulgidus |