Function
Commits PRPP to de novo purine-ring assembly.
A reusable pathway that assembles the purine ring on 5-phosphoribosyl diphosphate (PRPP) to form inosine monophosphate (IMP). The module represents ten ordered reaction positions and separates reaction roles from lineage-specific protein fusions. It includes alternative folate-dependent PurN and ATP/formate-dependent PurT routes for GAR formylation, and alternative two-enzyme and direct routes for AIR carboxylation. IMP-to-AMP and IMP-to-GMP branches are outside the module, although PurB also has a second physiological role in AMP synthesis.
All recommended fields populated.
✓ present
✓ every leaf node grounds to a representative protein.
✓ every declared conforms_to bundle matches its template motif.
16 complete review(s) · 4 with deep research · 10 missing review · 13 reviewed but lacking deep research
| Gene | Review | Complete | Deep research |
|---|---|---|---|
| ADSL P30566 | ✓ | 27/30 | ✗ |
| ATIC P31939 | ✓ | ✓ | ✗ |
| GART P22102 | ✓ | ✓ | ✗ |
| Escherichia coli PurM P08178 | ✗ | — | — |
| Escherichia coli PurN P08179 | ✗ | — | — |
| Escherichia coli PurK P09029 | ✗ | — | — |
| Escherichia coli PurB P0AB89 | ✗ | — | — |
| Escherichia coli PurF P0AG16 | ✗ | — | — |
| Escherichia coli PurE P0AG18 | ✗ | — | — |
| Escherichia coli PurL P15254 | ✗ | — | — |
| Escherichia coli PurH P15639 | ✗ | — | — |
| Escherichia coli PurD P15640 | ✗ | — | — |
| Escherichia coli PurT P33221 | ✗ | — | — |
| PAICS P22234 | ✓ | ✓ | ✗ |
| PFAS O15067 | ✓ | ✓ | ✗ |
| PPAT Q06203 | ✓ | ✓ | ✗ |
| purB Q88FR7 | ✓ | ✓ | ✗ |
| purC Q88NG9 | ✓ | ✓ | ✓ |
| purD Q88DK2 | ✓ | ✓ | ✓ |
| purE Q88C47 | ✓ | ✓ | ✗ |
| purF Q88LD5 | ✓ | ✓ | ✓ |
| purH Q88DK3 | ✓ | ✓ | ✗ |
| purK Q88C48 | ✓ | ✓ | ✗ |
| purL Q88P16 | ✓ | ✓ | ✗ |
| purM Q88MA9 | ✓ | ✓ | ✗ |
| purN Q88MB0 | ✓ | ✓ | ✓ |
| purT Q88MW1 | ✓ | ✓ | ✗ |
Exact UniProt exemplars delimit each reaction role without restricting the module taxonomically. A multidomain protein may satisfy more than one leaf: GART combines PurD-, PurN-, and PurM-like roles, PAICS combines direct AIR carboxylase and SAICAR synthetase roles, and PurH/ATIC commonly combines the final two reactions. GART remains an exact fusion exemplar on the PurD and PurN leaves, where its reviewed domain descriptions establish those activities without using its whole-protein family as a reaction selector. The PurM leaf uses PTHR10520:SF12 because that whole-protein subfamily contains both standalone bacterial PurM proteins and the GART fusion; the leaf molecular function constrains it to the shared cyclo-ligase role. Separate bacterial and eukaryotic adenylosuccinate-lyase families are retained for the PurB leaf. Parent PANTHER families containing both standalone enzymes and fusion proteins are selector scaffolds constrained by the leaf molecular function and exemplars. No ancestral PTN node is asserted without verified PAINT IBD evidence.
Commits PRPP to de novo purine-ring assembly.
Adds glycine to the growing purine precursor.
Uses a folate-bound one-carbon unit to form FGAR.
Uses free formate and ATP to form FGAR.
Introduces the second ring nitrogen to form FGAM.
Cyclizes FGAM to form the first purine-ring intermediate AIR.
Directly forms CAIR without a free N5-CAIR intermediate.
Adds aspartate to CAIR to form SAICAR.
Removes fumarate from SAICAR to form AICAR.
Adds the final folate-derived one-carbon unit.
Closes the second purine ring to produce IMP.