PurH is the bifunctional enzyme that completes de novo IMP synthesis. Its AICAR transformylase domain forms FAICAR using 10-formyltetrahydrofolate, and its IMP cyclohydrolase domain closes the purine ring to form IMP.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003937 IMP cyclohydrolase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Correct enzyme-specific molecular function. Reason: The exact Bifunctional purine biosynthesis protein PurH product assignment supports this activity. |
| GO:0004643 phosphoribosylaminoimidazolecarboxamide formyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Correct enzyme-specific molecular function. Reason: The exact Bifunctional purine biosynthesis protein PurH 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 either catalytic activity. 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. |
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Download this section (compressed HTML)Experiment: Test a clean purH deletion for purine auxotrophy and rescue by the appropriate downstream purine intermediate or by gene complementation.
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