| EC Tree |
| 2. Transferases |
| 2.7 Transferring phosphorus-containing groups |
| 2.7.8 Transferases for other substituted phosphate groups |
| ID: | 2.7.8.37 |
|---|---|
| Description: | Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase. |
| Cath: | 3.40.50.11310; |
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 2.7.8.37 |
| BRENDA Enzyme Link: | BRENDA 2.7.8.37 |
| KEGG Enzyme Link: | KEGG2.7.8.37 |
| BioCyc Enzyme Link: | BioCyc 2.7.8.37 |
| ExPASy Enzyme Link: | ExPASy2.7.8.37 |
| EC2PDB Enzyme Link: | EC2PDB 2.7.8.37 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.7.8.37 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.7.8.37 |
| IntEnz Enzyme Link: | IntEnz 2.7.8.37 |
| MEDLINE Enzyme Link: | MEDLINE 2.7.8.37 |
| RHEA:34679 | ATP + methylphosphonate = adenine + alpha-D-ribose 1-methylphosphonate 5-triphosphate |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[n;H0;+0:4](:[*:5]):[*:6].[*:7]-[OH;+0:8]>>[*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:8]-[*:7].[*:5]:[nH;+0:4]:[*:6] |
| Reaction | ![]() |
| Core-to-Core | |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Intermediates in the transformation of phosphonates to phosphate by bacteria. | Kamat SS, Williams HJ, Raushel FM | 2011 Nov 16 | 22089136 |