| EC Tree |
| 2. Transferases |
| 2.7 Transferring phosphorus-containing groups |
| 2.7.4 Phosphotransferases with a phosphate group as acceptor |
| ID: | 2.7.4.23 |
|---|---|
| Description: | Ribose 1,5-bisphosphate phosphokinase. |
| Alternative Name: |
Ribose 1,5-bisphosphokinase. |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 2.7.4.23 |
| BRENDA Enzyme Link: | BRENDA 2.7.4.23 |
| KEGG Enzyme Link: | KEGG2.7.4.23 |
| BioCyc Enzyme Link: | BioCyc 2.7.4.23 |
| ExPASy Enzyme Link: | ExPASy2.7.4.23 |
| EC2PDB Enzyme Link: | EC2PDB 2.7.4.23 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.7.4.23 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.7.4.23 |
| IntEnz Enzyme Link: | IntEnz 2.7.4.23 |
| MEDLINE Enzyme Link: | MEDLINE 2.7.4.23 |
| RHEA:20109 | alpha-D-ribose 1,5-bisphosphate + ATP = 5-phospho-alpha-D-ribose 1-diphosphate + ADP |
| RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Escherichia coli phnN, encoding ribose 1,5-bisphosphokinase activity (phosphoribosyl diphosphate forming): dual role in phosphonate degradation and NAD biosynthesis pathways. | Hove-Jensen B, Rosenkrantz TJ, Haldimann A, Wanner BL | 2003 May | 12700258 |