| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Paracidovorax citrulli | - |
- |
- |
| Paracidovorax citrulli KACC17005 | - |
- |
- |
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Chorismate | the bifunctional enzyme (cf. EC 4.2.1.51) possesses two distinct domains: chorismate mutase and prephenate dehydratase | Paracidovorax citrulli | Prephenate | - |
r | |
| Chorismate | the bifunctional enzyme (cf. EC 4.2.1.51) possesses two distinct domains: chorismate mutase and prephenate dehydratase | Paracidovorax citrulli KACC17005 | Prephenate | - |
r |
| Synonyms | Comment | Organism |
|---|---|---|
| Chorismate mutase/prephenate dehydratase | bifunctional enzyme, cf. EC 4.2.1.51 | Paracidovorax citrulli |
| CmpAc | bifunctional enzyme, cf. EC 4.2.1.51 | Paracidovorax citrulli |
| General Information | Comment | Organism |
|---|---|---|
| drug target | potential targets for developing virulence inhibitors against Acidovorax citrulli, a plant pathogenic bacterium that causes bacterial fruit blotch in cucurbit crops | Paracidovorax citrulli |
| malfunction | Acidovorax citrulli strain lacking the bifunctional chorismate mutase/prephenate dehydratase (CmpAc, cf. EC 4.2.1.51), are significantly less virulent on watermelon in the germinated seed inoculation and leaf infiltration assays. The strain shows reduced twitching halo production and enhanced biofilm formation. the strain is less tolerant to osmotic stress but more tolerant to antibiotics (polymyxin B) | Paracidovorax citrulli |
| physiological function | key enzyme in the shikimate pathway. It produces aromatic amino acids. Auxotrophic assays demonstrate that the bifunctional chorismate mutase/prephenate dehydratase (CmpAc, cf. EC 4.2.1.51) is required for the biosynthesis of phenylalanine, but not tyrosine. The comparative proteomic analysis revealed that CmpAc is mostly involved in cell wall/membrane/envelop biogenesis | Paracidovorax citrulli |