| Aspect | Summary |
|---|---|
| Gene/protein identity | **aroC**; UniProt **Q88LU7**; ordered locus **PP_1830**; organism **Pseudomonas putida** strain **KT2440**; annotated as a chorismate synthase family protein in the user-supplied UniProt record. Direct organism-specific primary literature on PP_1830 itself appears limited, so some functional details below are inferred from conserved chorismate synthase biochemistry and family-level evidence plus *P. putida* pathway-engineering studies (pqac-00000000, pqac-00000001, pqac-00000009). |
| Enzyme name / EC | **Chorismate synthase**; **EC 4.2.3.5**; terminal enzyme of the shikimate pathway in bacteria (pqac-00000000, pqac-00000001). |
| Reaction catalyzed | **5-enolpyruvylshikimate-3-phosphate (EPSP) → chorismate + phosphate**; mechanistically described as a **1,4-trans elimination** of phosphate from EPSP, creating the second double bond in the ring system of chorismate (pqac-00000000, pqac-00000001, pqac-00000002). |
| Required cofactor(s) | Requires **reduced FMN (FMNH2)** for activity even though the overall reaction is not net redox. In many bacterial/plant **monofunctional** enzymes, FMN is reduced externally (often by a separate flavin reductase or reduced flavin supply), whereas **bifunctional** enzymes in some fungi/protozoa can reduce FMN themselves with **NADPH** (pqac-00000000, pqac-00000001). |
| Pathway role | Catalyzes the **terminal step from EPSP to chorismate** in the shikimate pathway. **Chorismate** is the major branch-point precursor for **phenylalanine, tyrosine, tryptophan**, and additional metabolites such as **PABA/folate**, **ubiquinone/menaquinone-related products**, and other aromatic metabolites (pqac-00000000, pqac-00000001, pqac-00000010, pqac-00000015). |
| Quaternary structure notes | Chorismate synthase is commonly reported as a **tetramer**; structural work on non-*P. putida* orthologs describes a homotetramer or tetrameric assembly important for ligand binding/stability (pqac-00000002, pqac-00000003). |
| Likely localization | No direct localization evidence for **PP_1830/Q88LU7** was retrieved here. Given its role in central aromatic biosynthesis and lack of membrane-targeting evidence in the gathered sources, the enzyme is most reasonably treated as a **cytosolic bacterial metabolic enzyme**, but this point should be considered an inference rather than a directly sourced *P. putida* measurement. |
| *P. putida* application: PHBA production | In *P. putida* KT2440, shikimate/chorismate flux was engineered toward **para-hydroxybenzoic acid (PHBA)** by expressing **E. coli ubiC** and feedback-resistant **aroG D146N**, with deletions of **pobA, pheA, trpE**, and **hexR**. Best reported performance: **1.73 g/L PHBA** and **18.1% C-mol/C-mol** carbon yield in non-optimized fed-batch fermentation (pqac-00000004, pqac-00000007). |
| *P. putida* application: pABA production / aroC tuning | A 2024 combinatorial-expression study in *P. putida* found **pABA titers spanning ~2–232 mg/L**. **High aroC overexpression** was reported to have an unfavorable or only mildly beneficial effect; the authors concluded **mild rather than maximal aroC expression** was preferable, while **aroB** emerged as a stronger bottleneck (pqac-00000005, pqac-00000009). |
| *P. putida* application: gallic acid production | Engineering of shikimate-pathway flux in *P. putida* KT2440 for **gallic acid** production from glycerol achieved **346.7 ± 0.004 mg/L** gallic acid and an observed yield of **0.12 g/g glycerol**; this study did not specifically manipulate aroC, but it demonstrates practical importance of chorismate-pathway flux control in this host (pqac-00000006). |


*Table: This table summarizes the verified identity, core enzymology, pathway context, and recent Pseudomonas putida engineering relevance of aroC/chorismate synthase. It is useful as a compact evidence-backed reference for the final research report.*