A0A0B4LFV5 is the 174 aa PB isoform, independently linked by FlyBase to FBpp0309413. The same-gene comparison supports a native short isoform, not wrong sequence. DUF1091 and a signal peptide provide fold/localization leads without identifying a molecular activity.
The enzyme-activator prediction remains UNC because no specific enzyme partner or activation mechanism is established. The ganglioside-catabolism prediction is NPI/PATHWAY_CONTEXT_IGNORED: PMID:29844375(https://pubmed.ncbi.nlm.nih.gov/29844375/) reports undetectable endogenous gangliosides and engineered reconstitution in flies. The study distinguishes fly mactosylceramide metabolism from the mammalian lactosylceramide/ganglioside pathway. This is not a blanket claim that flies lack sialic acid: glycoprotein sialylation is distinct. The claim under review is a native evolved pathway, not possible turnover of experimentally introduced gangliosides. Human P17900 and macaque Q8HXX6 donor source records are retained.
All three ND GOA root rows remain non-core unknown markers. No speculative positive core molecular function is added. The full original prediction JSON preserves all TM-align scores and source identifiers.
The Falcon synthesis finds no target-specific biochemical function and distinguishes CG33453 from the separate DUF1091 genes daedalus and decima. Its CheA/CheB family discussion suggests secreted chemical-signal handling but does not establish enzyme activation or ganglioside turnover. Exact PB identity and signal-peptide evidence are independently recorded locally; the published endogenous-ganglioside constraint remains the basis for the negative process assessment.