CG8745

UniProt ID: Q9VU95
Organism: Drosophila melanogaster
Review Status: IN PROGRESS
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Gene Description

CG8745 is a 494-residue class-III pyridoxal-phosphate-dependent enzyme related to ethanolamine-phosphate phospho-lyase/AGXT2L proteins. Its major and small PLP-enzyme domains support cofactor-dependent amino-compound metabolism. The precise physiological substrate and intracellular compartment in Drosophila remain unresolved; its historical aminotransferase-like name does not establish conventional aminotransferase activity.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0030170 pyridoxal phosphate binding
IEA
GO_REF:0000002
ACCEPT
Summary: A PLP-dependent catalytic fold supports cofactor binding.
Reason: CG8745 retains the major and small class-III PLP-dependent enzyme domains and the PLP attachment-site signature. This supports cofactor binding while leaving physiological substrate specificity distinct from the historical aminotransferase-like name.
Supporting Evidence:
file:DROME/CG8745/CG8745-uniprot.txt
aminotransferase family. {ECO:0000305}.
GO:0035094 response to nicotine
IEP
PMID:17237783
Quantitative trait transcripts for nicotine resistance in Dr...
UNDECIDED
Summary: The nicotine expression association is not resolved at the target level.
Reason: The accessible study reports transcript associations with nicotine resistance and emphasizes ornithine aminotransferase. Its abstract does not identify the CG8745 assay, and the target-specific expression result requires the full gene table. This is not evidence of misattribution and does not establish nicotine metabolism by CG8745.
Supporting Evidence:
PMID:17237783
We performed a scan for such quantitative trait transcripts in adult female heads of the fruit fly (Drosophila melanogaster) that might explain variation for nicotine resistance.
GO:0050459 ethanolamine-phosphate phospho-lyase activity
ISS
GO_REF:0000024
UNDECIDED
Summary: Ethanolamine-phosphate phospho-lyase is a plausible ortholog-based reaction.
Reason: The ISS source is human Q8TBG4/ETNPPL, and the target has the corresponding PLP-enzyme architecture. However, broad class-III domain membership and absence of conventional aminotransferase activity alone do not establish phosphoethanolamine turnover by CG8745; the donor biochemical evidence and fly substrate selectivity must be distinguished.
Supporting Evidence:
file:DROME/CG8745/CG8745-uniprot.txt
aminotransferase family. {ECO:0000305}.
file:DROME/CG8745/CG8745-uniprot.txt
Does not seem to possess aminotransferase activity.

Core Functions

Binds the PLP cofactor through a conserved class-III enzyme architecture; the specific physiological reaction remains unresolved.

Molecular Function:
pyridoxal phosphate binding
Supporting Evidence:
  • file:DROME/CG8745/CG8745-uniprot.txt
    aminotransferase family. {ECO:0000305}.

References

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Deep Research

Falcon

(CG8745-deep-research-falcon.md)

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