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Literature summary for 5.3.2.5 extracted from
- A functional link between RuBisCo-like protein of Bacillus and photosynthetic RuBisCo (2003), Science, 302, 286-290.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | a growth-defective mutant, in which the gene for the RLP is disrupted, is rescued by the gene for RuBisCO from the photosynthetic bacterium Rhodospirillum rubrum | Bacillus subtilis |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Bacillus subtilis |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5-(methylthio)-2,3-dioxopentyl phosphate | Bacillus subtilis | - |
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate | - |
? | |
| additional information | Bacillus subtilis | RLP has no RuBP-carboxylating activity, RLP catalyzes the DK-MTP-1-P enolase reaction and not the enolase/phosphatase reaction | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5-(methylthio)-2,3-dioxopentyl phosphate | - |
Bacillus subtilis | 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate | - |
? | |
| additional information | RLP has no RuBP-carboxylating activity, RLP catalyzes the DK-MTP-1-P enolase reaction and not the enolase/phosphatase reaction | Bacillus subtilis | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| RLP | - |
Bacillus subtilis |
| RuBisCO-like protein | - |
Bacillus subtilis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Bacillus subtilis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Bacillus subtilis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | phylogenetic tree of RuBisCO and RLPs, overview. The RLP of Bacillus subtilis includes both those amino acid residues of RuBisCO that are responsible for binding the phosphate on C1 of RuBP and those required for activation by CO2. However, the residues of RuBisCO that are responsible for binding the other phosphate group of RuBP and the residues of loop 6, which are essential for RuBisCO activity are replaced by different amino acids in RLP | Bacillus subtilis |
| malfunction | a growth-defective mutant, in which the gene for this RLP is disrupted, is rescued by the gene for RuBisCO from the photosynthetic bacterium Rhodospirillum rubrum, the photosynthetic RuBisCO from Rhodospirillum rubrum retains the ability to function in the methionine salvage pathway in Bacillus subtilis | Bacillus subtilis |
| metabolism | the RuBisCO-like protein catalyzes the 2,3-diketo-5-methylthiopentyl-1-phosphate enolase reaction in the methionine salvage pathway | Bacillus subtilis |
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Release 2023.1 (January 2023)
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