PurL is the large-type phosphoribosylformylglycinamidine synthase that uses glutamine and ATP to convert FGAR to FGAM during de novo IMP synthesis.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004642 phosphoribosylformylglycinamidine synthase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Correct enzyme-specific molecular function. Reason: The exact Phosphoribosylformylglycinamidine synthase product assignment supports this activity. |
| GO:0005524 ATP binding | IEA GO_REF:0000104 | KEEP AS NON CORE | Summary: Valid substrate binding, but not the core function of PurL. Reason: ATP is consumed by the synthase reaction, while the enzyme-specific activity captures the core function. |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Plausible electronic localization that is not core to the enzyme function. Reason: Cytoplasm is consistent with a soluble bacterial metabolic enzyme, but no direct localization evidence was found. |
| GO:0006164 purine nucleotide biosynthetic process | IEA GO_REF:0000120 | MODIFY | Summary: Correct but broader than the specific pathway assignment. Reason: Replace the broad purine-nucleotide process with de novo IMP biosynthesis. Proposed replacements: 'de novo' IMP biosynthetic process |
| GO:0006189 'de novo' IMP biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: Correct pathway assignment. Reason: This enzyme catalyzes a required reaction between PRPP and IMP. |
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Download this section (compressed HTML)Experiment: Test a clean purL deletion for purine auxotrophy and rescue by the appropriate downstream purine intermediate or by gene complementation.
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