Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on Enzyme Commission mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
TreeGrafter-generated GO annotations
UniProt entry A0A2H4GSI3 for Nicotiana attenuata UGT85A2_0
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UGT85A2_0 is a UDP-glycosyltransferase family enzyme
"CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family."
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The public UniProt entry carries family-derived glucosyltransferase annotations
"DE RecName: Full=7-deoxyloganetic acid glucosyltransferase"
NaUGT1 UGT85A2_0 candidate notes
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UGT1 is the NaGT step in the reconstituted nicotine synthase cascade
"The glucosylation preprint makes UGT1 a core late-pathway enzyme by reconstituting the four-enzyme nicotine synthase cascade with UGT1, A622, BBLa, and beta-GD1, and it explicitly assigns UGT1 = NaGT, the nicotinic acid N-glucosyltransferase step."
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UGT85A2_0 is the best current sequence-backed NICAT ortholog to tobacco UGT1
"The 2026-04-05 mapping dive assigns NaUGT1 to UGT85A2_0 / A0A2H4GSI3 as the best current sequence-backed NICAT ortholog to tobacco UGT1."
Deep research report on NaUGT1/UGT85A2_0 (Falcon/Edison Scientific Literature)
Blinded OpenScientist function-assignment report (TreeGrafter audit)
Existing falcon function-hypothesis report
Nicotine biosynthesis is completed by cryptic activating glucosylation.
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The purified tobacco UGT1 enzyme N-glucosylates nicotinic acid and participates in the reconstituted nicotine biosynthesis cascade. Supplementary sequences explicitly identify the assayed homolog.
"producing nicotinic acid N-glucoside ( 10)
from nicotinic acid ( 2) and UDP-glucose"
Complete biosynthesis of nicotine.
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The independent N. attenuata study biochemically assays NaUGT1 and disrupts its locus; primary supplemental primers link those assays to g26396, with an N-terminal construct extension documented in the identity analysis.
"Abrogating any of these components depletes nicotine accumulations."
Qualitative and Quantitative NAD(+) Metabolomics Lead to Discovery of Multiple Functional Nicotinate N-Glycosyltransferase in Arabidopsis.
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Arabidopsis UGT76C4/UGT76C5 are experimentally characterized nicotinate N-glycosyltransferases, contradicting the report claim that no plant examples were known.
"Previously, we had identified UGT76C4 and UGT76C5 as NA N-glucosyltransferase"
Reproducible NaUGT1 primary-sequence and ontology reconciliation
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Explicit primary accession mapping and an independently recomputed global alignment support the close tobacco homolog; the gene-level Cell evidence resolves the candidate identity.
"The assayed tobacco UGT1 maps explicitly to A0A1S3YWH6 and is a nicotinate N-glucosyltransferase."
Cell 2026 NaUGT1 identity check against primary primers and GenBank sequences
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Published cloning and perturbation primers map to the g26396 locus represented by A0A2H4GSI3; a primer-compatible extended ORF contains its entire 485-aa sequence unchanged.
"Figure 3D assays purified recombinant NaUGT1 expressed in E. coli and detects nicotinic acid N-glucoside from nicotinic acid."
OpenScientist adjudication of NaUGT1 identity and nicotinate glucosylation
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The report claims nicotinate N-glucosylation is outside nicotine biosynthesis.
"nicotinic acid *N*-glucoside is a separate conjugation/storage branch (one of three fates of nicotinic acid), not a nicotine-biosynthetic step."