CG18547 is a 345-residue aldo-keto-reductase-family protein with an NADP-dependent oxidoreductase domain. Its architecture supports a redox function, but the physiological carbonyl substrate is unresolved. Specific assignments to L-galactose oxidation or D-arabinonolactone biosynthesis require evidence beyond the shared AKR fold.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0010349 L-galactose dehydrogenase activity | IEA GO_REF:0000002 | UNDECIDED | Summary: L-galactose substrate specificity is not resolved by the AKR domain. Reason: The exact target contains an NADP-dependent oxidoreductase/aldo-keto-reductase domain, but these enzymes accommodate diverse carbonyl substrates. The family assignment does not establish L-galactose dehydrogenase activity in fly. Supporting Evidence: file:DROME/CG18547/CG18547-uniprot.txt /note="NADP-dependent oxidoreductase" file:DROME/CG18547/CG18547-uniprot.txt DR Pfam; PF00248; Aldo_ket_red; 1. |
| GO:0016491 oxidoreductase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Broad oxidoreductase activity is a defensible AKR-family inference. Reason: The full aldo-keto-reductase domain and curated PAINT placement support the broad redox function, while neither the generic name nor the domain resolves the physiological sugar or steroid substrate. Supporting Evidence: file:DROME/CG18547/CG18547-uniprot.txt /note="NADP-dependent oxidoreductase" file:DROME/CG18547/CG18547-uniprot.txt DR Pfam; PF00248; Aldo_ket_red; 1. |
| GO:0016491 oxidoreductase activity | IEA GO_REF:0000002 | ACCEPT | Summary: Broad oxidoreductase activity is a defensible AKR-family inference. Reason: The full aldo-keto-reductase domain and curated PAINT placement support the broad redox function, while neither the generic name nor the domain resolves the physiological sugar or steroid substrate. Supporting Evidence: file:DROME/CG18547/CG18547-uniprot.txt /note="NADP-dependent oxidoreductase" file:DROME/CG18547/CG18547-uniprot.txt DR Pfam; PF00248; Aldo_ket_red; 1. |
| GO:0070485 dehydro-D-arabinono-1,4-lactone biosynthetic process | ISS GO_REF:0000024 | UNDECIDED | Summary: Dehydro-D-arabinonolactone synthesis requires a specific substrate/pathway assignment. Reason: The broad AKR fold supports carbonyl chemistry but does not establish the annotated D-arabinose-associated pathway. The inherited ISS process requires substrate-specific biochemical support distinct from the L-galactose electronic annotation. Supporting Evidence: file:DROME/CG18547/CG18547-uniprot.txt /note="NADP-dependent oxidoreductase" file:DROME/CG18547/CG18547-uniprot.txt DR Pfam; PF00248; Aldo_ket_red; 1. |
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