1 Parent Features
| DB identifier | Type | Name |
|---|---|---|
| IPR015813 | Domain | Pyruvate/Phosphoenolpyruvate kinase-like domain |
| Type: | Domain | Name: | Phosphoenolpyruvate phosphomutase, core |
| Description: | Phosphonates are a class of organophosphorus compounds, characterised by a stable C-P bond, which are found in a variety of biologically produced molecules including antiobiotics, lipids, proteins and polysaccharides []. The functions of these molecules include phosphorus storage, cell communication, host recognition and chemical warfare. Phosphoenolpyruvate (PEP) phosphomutase catalyses the reversible conversion of PEP to 3-phosphonopyruvate, forming a stable C-P bond, which is the entry point to all known phosphonate biosynthetic pathways [].This entry consists of characterised and predicted PEP phosphomutases found in bacterial and eukayotic species. A closely related enzyme, phosphonopyruvate hydrolase from Variovorax sp. Pal2, is excluded from this entry, and the functional identification of some more distantly related sequences, such as from Bacteroides fragilis, Treponema denticola, and Clostridium tetani E88is unknown.PEP phosphomutase forms a modified TIM barrel fold where the eighth alpha helix adopts a different conformation than in the classical TIM barrel fold []. The substrate binds in the central channel of the barrel and is anchored to the active site by the Mg(2+) cofactor []. In the absence of substrate the active site is acessible to the solvent, while substrate-binding causes a conformational change where a large loop shields the site from solvent []. This shielding appears to be required for catalysis to occur. | Short Name: | PEnolPyrv_PMutase_core |
| DB identifier | Type | Name |
|---|---|---|
| IPR015813 | Domain | Pyruvate/Phosphoenolpyruvate kinase-like domain |
