PurC is SAICAR synthetase, the ATP-dependent enzyme that condenses CAIR with aspartate to form SAICAR during de novo IMP synthesis.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004639 phosphoribosylaminoimidazolesuccinocarboxamide synthase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Correct enzyme-specific molecular function. Reason: The exact Phosphoribosylaminoimidazole-succinocarboxamide synthase product assignment supports this activity. |
| GO:0005829 cytosol | IEA GO_REF:0000118 | KEEP AS NON CORE | Summary: Plausible electronic localization that is not core to the enzyme function. Reason: Cytosol is consistent with a soluble bacterial metabolic enzyme, but no direct localization evidence was found. |
| GO:0006164 purine nucleotide biosynthetic process | IEA GO_REF:0000002 | 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. |
| GO:0009236 cobalamin biosynthetic process | IEA GO_REF:0000002 | REMOVE | Summary: Unsupported pathway transfer from a broad enzyme-family mapping. Reason: Canonical PurC catalyzes SAICAR formation in purine synthesis; no cobalamin role is supported. Supporting Evidence: file:PSEPK/purC/purC-uniprot.txt RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase |
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Download this section (compressed HTML)Q: Should the cobalamin-process InterPro mapping be narrowed so it is not transferred to canonical PurC proteins?
Experiment: Test a clean purC deletion for purine auxotrophy and rescue by the appropriate downstream purine intermediate or by gene complementation.
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Download this section (compressed HTML)GO:0006189.Loading supporting contentβ¦
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