NaAO2_candidate_AO_1 is the second current NICAT L-aspartate oxidase candidate for the duplicated pyridine branch that feeds nicotine biosynthesis. Like AO_0, it is a bona fide chloroplast-localized NadB-family enzyme, but current public evidence still does not distinguish it as the specialized pathway paralog.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0008734 L-aspartate oxidase activity | IEA GO_REF:0000120 | ACCEPT | Summary: This specific catalytic activity fits AO_1 well. Reason: AO_1 is clearly an L-aspartate oxidase family member rather than only a generic oxidoreductase. Supporting Evidence: file:NICAT/NaAO2_candidate_AO_1/NaAO2_candidate_AO_1-notes.md UniProt curates A0A314LIN0 as an L-aspartate oxidase/NadB-family flavoprotein that catalyzes oxidation of L-aspartate to iminoaspartate, placing it in the same upstream NAD-derived chemistry that can feed pyridine alkaloid biosynthesis. |
| GO:0009435 NAD+ biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: AO_1 belongs in NAD biosynthesis. Reason: AO family chemistry feeds the de novo NAD branch from which the nicotine pyridine branch evolved. Supporting Evidence: file:NICAT/NaAO2_candidate_AO_1/NaAO2_candidate_AO_1-notes.md UniProt curates A0A314LIN0 as an L-aspartate oxidase/NadB-family flavoprotein that catalyzes oxidation of L-aspartate to iminoaspartate, placing it in the same upstream NAD-derived chemistry that can feed pyridine alkaloid biosynthesis. |
| GO:0009507 chloroplast | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Chloroplast localization is supported but not central to the paralog-resolution question. Reason: Retain the location as plausible contextual information while keeping the main review emphasis on pathway assignment. Supporting Evidence: file:NICAT/NaAO2_candidate_AO_1/NaAO2_candidate_AO_1-uniprot.txt CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast |
| GO:0016491 oxidoreductase activity | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: This generic parent term adds little beyond the specific catalytic annotation. Reason: GO:0008734 already captures the informative chemistry for this candidate. Supporting Evidence: file:NICAT/NaAO2_candidate_AO_1/NaAO2_candidate_AO_1-notes.md UniProt curates A0A314LIN0 as an L-aspartate oxidase/NadB-family flavoprotein that catalyzes oxidation of L-aspartate to iminoaspartate, placing it in the same upstream NAD-derived chemistry that can feed pyridine alkaloid biosynthesis. |
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Download this section (compressed HTML)Q: Is AO_1 transcription or protein abundance more tightly coupled to nicotine induction than AO_0?
Q: Do AO_1 and AO_0 make redundant or distinct contributions to the pyridine precursor pool in roots?
Experiment: Measure AO_1 and AO_0 expression and coexpression with established nicotine genes after topping, jasmonate, and herbivory treatments.
Hypothesis: One of the two AO paralogs is more tightly integrated into the nicotine pathway regulatory program.
Type: expression profiling
Experiment: Compare the metabolic impact of AO_1 and AO_0 perturbation on quinolinate-, nicotinate-, and nicotine-related metabolites.
Hypothesis: Only one AO paralog has a major effect on nicotine precursor flux.
Type: genetics plus metabolite profiling
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