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.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0016407 acetyltransferase activity | IEA GO_REF:0000104 | ACCEPT | Summary: 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. Supporting Evidence: 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. |
| GO:0016740 transferase activity | IEA GO_REF:0000104 | MODIFY | Summary: The GNAT domain supports acetyltransferase activity as a more informative family-level function than generic transferase or acyltransferase activity. The acceptor substrate remains unresolved. Proposed replacements: acetyltransferase activity Supporting Evidence: 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. |
| GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups | IEA GO_REF:0000002 | MODIFY | Summary: The GNAT domain supports acetyltransferase activity as a more informative family-level function than generic transferase or acyltransferase activity. The acceptor substrate remains unresolved. Proposed replacements: acetyltransferase activity Supporting Evidence: 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. |
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