NCU12035: biological evidence

NCU12035 is a predicted GNAT-family acetyltransferase with an acyl-CoA-binding fold. It is expected to transfer an acetyl group to an unidentified acceptor. Its substrate class, physiological pathway, and cellular location remain unresolved; the shared GNAT fold encompasses enzymes that modify proteins and diverse small molecules.

• acetyltransferase activity: The complete GNAT acetyltransferase domain supports broad acetyl-transfer chemistry. Primary classification of eukaryotic GNATs documents the shared acyl-CoA-dependent catalytic scaffold but substantial substrate diversity; no particular acceptor is assigned here.
• transferase activity: The GNAT domain supports acetyltransferase activity as a more informative family-level function than generic transferase or acyltransferase activity. The acceptor substrate remains unresolved.
• acyltransferase activity, transferring groups other than amino-acyl groups: The GNAT domain supports acetyltransferase activity as a more informative family-level function than generic transferase or acyltransferase activity. The acceptor substrate remains unresolved.

Primary evidence excerpts

• [file:NEUCR/NCU12035/NCU12035-uniprot.txt] “DR InterPro; IPR000182; GNAT_dom.”
• PMID:33362253 “GNAT enzymes transfer an acyl moiety from acyl coenzyme A to a
  wide range of substrates including aminoglycosides, serotonin,
  glucosamine-6-phosphate, protein N-termini and lysine residues of histones and
  other proteins.”

Provenance: live API snapshot 2026-09-09T03:00:51.831347+00:00. Complete API prediction JSON and all emitted claim IDs, text, and original evidence are preserved in the source and provenance JSON files. Current sequence/annotation data are separate comparison snapshots. Annotation overlap records known biology, not demonstrated training membership. All seven gene-focused Falcon jobs completed; the provider reports were inspected and useful primary leads checked. Publication retrieval used Europe PMC metadata/XML when the canonical PubMed fetch returned HTTP 429.