PchA (PA4231) is the isochorismate synthase of Pseudomonas aeruginosa, the first enzyme of the pathway that makes salicylate and the siderophore pyochelin. Encoded as the last gene of the iron-repressed pchDCBA operon, it is a 52-kDa Mg2+-dependent monomer of the chorismate-utilizing enzyme family that converts chorismate to isochorismate; the isochorismate pyruvate-lyase PchB then converts isochorismate to salicylate and pyruvate. PchA is rate-limiting for salicylate formation, and its cellular concentration, set at the transcriptional level by iron (negative) and pyochelin (positive), controls flux into pyochelin biosynthesis.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0008909 isochorismate synthase activity | IBA GO_REF:0000033 | ACCEPT | Summary: IBA from PTN000132907 (isochorismate synthase clade, 2 seeds, 17 leaf IBAs). Seeds are E. coli EntC (P0AEJ2, IDA/EXP) and PchA itself (PseudoCAP IDA, PMID:12624097). Reason: PchA has its own purified-enzyme kinetics for this activity, and the node term suits an isochorismate synthase clade; the IBD would stand on E. coli EntC alone. Supporting Evidence: PMID:12624097 At pH 7.0, the optimum, a K(m) = 4.5 microm and a k(cat) = 43.1 min(-1) were determined for chorismate. |
| GO:0008909 isochorismate synthase activity | IDA PMID:12624097 Isochorismate synthase (PchA), the first and rate-limiting e... | ACCEPT | Summary: PseudoCAP IDA, the PTN000132907 seed row. PchA was purified to homogeneity from P. aeruginosa and its Mg2+-dependent kinetics with chorismate were determined. Reason: Seed verdict SOUND; direct assay of the purified gene product. Supporting Evidence: PMID:12624097 The PchA protein was purified to apparent electrophoretic homogeneity from a PchA-overexpressing P. aeruginosa strain. PMID:12624097 At pH 7.0, the optimum, a K(m) = 4.5 microm and a k(cat) = 43.1 min(-1) were determined for chorismate. |
| GO:0008909 isochorismate synthase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Combined automated isochorismate synthase activity. Reason: Same claim as the IDA row. Supporting Evidence: PMID:12624097 At pH 7.0, the optimum, a K(m) = 4.5 microm and a k(cat) = 43.1 min(-1) were determined for chorismate. |
| GO:0009697 salicylic acid biosynthetic process | IDA PMID:7500944 Structural genes for salicylate biosynthesis from chorismate... | ACCEPT | Summary: Salicylate formation from chorismate required pchA together with pchB, in an E. coli entC mutant and in extracts with overproduced PchA and PchB. Reason: PchA catalyses the first of the two steps from chorismate to salicylate, so it does part of the work of the process. Supporting Evidence: PMID:7500944 Our results are consistent with a pathway leading from chorismate to isochorismate and then to salicylate plus pyruvate, catalyzed consecutively by the iron-repressible PchA and PchB proteins in P. aeruginosa. |
| GO:0009697 salicylic acid biosynthetic process | IEA GO_REF:0000041 | ACCEPT | Summary: UniPathway salicylate biosynthesis. Reason: Same claim as the IDA row. Supporting Evidence: PMID:7500944 Our results are consistent with a pathway leading from chorismate to isochorismate and then to salicylate plus pyruvate, catalyzed consecutively by the iron-repressible PchA and PchB proteins in P. aeruginosa. |
| GO:0042864 pyochelin biosynthetic process | IDA PMID:12624097 Isochorismate synthase (PchA), the first and rate-limiting e... | ACCEPT | Summary: PchA is the first enzyme of the pyochelin pathway; overexpressing pchA raised both salicylate and pyochelin production. Reason: PchA catalyses the committed first step of pyochelin biosynthesis (chorismate to isochorismate), so it takes part in the process. Supporting Evidence: PMID:12624097 In cultures grown in iron-limiting media to high cell densities, overexpression of the pchA gene resulted in overproduction of salicylate as well as in enhanced pyochelin formation. |
Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)