Cloned (Comment) | Organism |
---|---|
gene rbcLIV, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, cloning in Escherichia coli strain JM109, expression in Escherichia coli strain BL21 | Microcystis aeruginosa |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Microcystis aeruginosa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
5-methylthio-2,3-dioxo-pentyl phosphate | Microcystis aeruginosa | purified recombinant rubisco-like protein RbcLIV, overexpressed in Escherichia coli cells, does not display CO2 fixation activity but catalyzes enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate | 2-hydroxy-5-methylthio-3-oxopentenyl phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Microcystis aeruginosa | - |
planktonic organism | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
5-methylthio-2,3-dioxo-pentyl phosphate | purified recombinant rubisco-like protein RbcLIV, overexpressed in Escherichia coli cells, does not display CO2 fixation activity but catalyzes enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate | Microcystis aeruginosa | 2-hydroxy-5-methylthio-3-oxopentenyl phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | RbcLIV secondary structure analysis, spectroscopic analysis, and three-dimensional structure modeling, overview | Microcystis aeruginosa |
Synonyms | Comment | Organism |
---|---|---|
RuBisCO-like protein | - |
Microcystis aeruginosa |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Microcystis aeruginosa |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Microcystis aeruginosa |
General Information | Comment | Organism |
---|---|---|
evolution | members of the form IV subfamily, Rubisco-like proteins or RLPs, do not display Rubisco activity, but the two eubacterial members of this family play a role in sulfur metabolism. Discovery of the coexistence of RbcLI and RbcLIV in cyanobacteria, the ancestors of chloroplasts, enlightens episodes of the chaotic evolutionary history of the Rubiscos, a protein family of major importance for life on earth | Microcystis aeruginosa |
additional information | the rbcLIV gene rescues a Bacillus subtilis MtnW-deficient mutant | Microcystis aeruginosa |