PurD is phosphoribosylamine--glycine ligase, the ATP-dependent enzyme that adds glycine to 5-phosphoribosylamine to form GAR in the second reaction of de novo IMP synthesis.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003824 catalytic activity | IEA GO_REF:0000117 | MODIFY | Summary: Correct but less informative than the enzyme-specific activity. Reason: Replace the generic catalytic parent with phosphoribosylamine-glycine ligase activity. Proposed replacements: phosphoribosylamine-glycine ligase activity |
| GO:0004637 phosphoribosylamine-glycine ligase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Correct enzyme-specific molecular function. Reason: The exact Phosphoribosylamine--glycine ligase product assignment supports this activity. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Valid substrate binding, but not the core function of PurD. Reason: ATP is consumed by the ligase reaction, while the enzyme-specific activity captures the core function. |
| 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:0009113 purine nucleobase biosynthetic process | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: Nucleobase-process annotation does not match the nucleotide product of this pathway. Reason: The PRPP-to-IMP pathway produces a purine nucleotide, not a free purine nucleobase; GO:0009113 is therefore not a broader parent of GO:0006189. |
| GO:0046872 metal ion binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Valid cofactor binding, but not the core function of PurD. Reason: Metal binding supports catalysis, while the enzyme-specific activity captures the core function. |
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Download this section (compressed HTML)Experiment: Test a clean purD 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:0004637. ATP and metal binding are validGO:0006189.Loading supporting contentβ¦
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