CG5611

UniProt ID: Q9VB17
Organism: Drosophila melanogaster
Review Status: DRAFT
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Gene Description

CG5611 encodes a 326-residue protein with a single crotonase-fold (enoyl-CoA hydratase/isomerase-like, PF00378) domain spanning residues 47-290. It belongs to PANTHER subfamily PTHR43802:SF1, whose members include the Drosophila paralog Srlp (CG5844) and bacterial enzymes with chemically distinct activities, including carbon-carbon bond-cleaving hydrolases. CG5611 keeps the oxyanion-hole glycine and the first catalytic glutamate of the crotonase fold, but the second catalytic glutamate of canonical enoyl-CoA hydratase appears to be replaced by asparagine. Its reaction, substrate, subcellular location and physiological role have not been determined experimentally; the only gene-specific data are from a large-scale RNAi behavioural screen.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0003674 molecular_function
ND
GO_REF:0000015 		ACCEPT
Summary: No molecular function has been demonstrated for CG5611, and the family evidence is not specific enough to assign one.
Reason: The crotonase fold establishes family membership but not a reaction. PTHR43802:SF1 holds enzymes with different chemistries (6-oxocamphor and 6-oxocyclohexene-carbonyl-CoA hydrolases, as well as predicted hydratases). No human or mouse ortholog lies in this PANTHER family, and the second catalytic glutamate of canonical enoyl-CoA hydratase appears to be replaced by asparagine in CG5611. The literature search found no biochemical study, so the ND placeholder stands.
Supporting Evidence:
file:DROME/CG5611/CG5611-deep-research-falcon.md
However, no CG5611-specific biochemical study was found that identifies a reaction, substrate, product, kinetic parameters, catalytic residues, pathway, or intracellular compartment.
file:DROME/CG5611/CG5611-bioinformatics/RESULTS.md
The exact reaction remains unresolved
GO:0005575 cellular_component
ND
GO_REF:0000015 		ACCEPT
Summary: No experimental localization exists for CG5611.
Reason: The fly paralog Srlp in the same PANTHER subfamily has an IDA mitochondrial matrix annotation, and the N-terminus of CG5611 is arginine-rich. Neither establishes that CG5611 is mitochondrial, and no targeting analysis or localization experiment for CG5611 is available. The ND placeholder stands.
Supporting Evidence:
file:DROME/CG5611/CG5611-deep-research-falcon.md
CG5611's functional compartment is **unknown**.
GO:0008150 biological_process
ND
GO_REF:0000015 		ACCEPT
Summary: No biological process has been established for CG5611.
Reason: The reaction is unknown, so no metabolic process can be assigned. The olfactory-conditioning screen hit (Walkinshaw et al. 2015) is a confounded RNAi phenotype and does not show that the protein takes part in memory formation, so it does not justify a process annotation.
Supporting Evidence:
file:DROME/CG5611/CG5611-deep-research-falcon.md
Consequently, no specific biochemical pathway can presently be assigned to CG5611 with high confidence.

References

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Suggested Questions for Experts

Q: Does CG5611 retain hydratase or isomerase activity on any 2- or 3-enoyl-CoA, given that the second catalytic glutamate of canonical enoyl-CoA hydratase appears to be replaced by asparagine?

Q: Is CG5611 targeted to the mitochondrial matrix like its PTHR43802:SF1 paralog Srlp (CG5844), and is its arginine-rich N-terminus a cleaved targeting presequence?

Suggested Experiments

Experiment: Express recombinant CG5611 and screen enoyl-CoA, 3-enoyl-CoA and beta-ketoacyl/oxo CoA-thioester substrates of different chain lengths, identifying products by LC-MS/MS. Test the N171E and E151Q mutants to establish which acid/base residues the reaction needs.

Type: enzyme activity assay

Experiment: Tag endogenous CG5611 and co-stain with mitochondrial and peroxisomal markers, then confirm the location by subcellular fractionation and protease-protection assays.

Type: subcellular localization

External Prediction Reviews

These computational predictions are reviewed separately from the GOA annotation set used for this review. The assessments below are from this project and do not constitute official GO annotations or endorsement by GO/UniProt. They are not included in the existing annotation review above.

ProtNLM External predictions

View prediction review YAML · CG5611-protnlm-predictions-review.yaml · Review status: COMPLETE

The ProtNLM2 API snapshot retrieved 2026-09-08 contains no GO-term predictions for Q9VB17. CG5611 carries a single enoyl-CoA hydratase/isomerase-like (crotonase-fold, PF00378) domain and is classified in PANTHER subfamily PTHR43802:SF1, a subfamily that groups enzymes of chemically distinct activities, so membership does not identify a reaction. CG5611 retains the oxyanion-hole glycine and the first catalytic glutamate, but the position of the second catalytic glutamate of canonical enoyl-CoA hydratase is an asparagine, and no human or mouse protein lies in this PANTHER family to serve as a characterized ortholog. A PubMed search for CG5611 returned no articles, and no biochemical, localization or pathway study of the protein exists. The gene carries only ND root annotations for all three aspects, which record this lack of evidence rather than missing positive predictions. No catalytic, fatty-acid oxidation, mitochondrial or other specific GO term is supported, so the absence of ProtNLM2 GO output is an appropriate outcome and no omission is scored. The separate tentative FUNCTION narrative about fatty-acid oxidation and mitochondrial localization is assessed in the linked function review and remains unsupported. This completed record assesses the absence of GO output; predictions is empty because no GO or EC prediction was emitted.

Source documents: genes/DROME/CG5611/CG5611-predictions-source.json · projects/PROTNLM_EVALUATION/fly-benchmark/manifest.json · genes/DROME/CG5611/CG5611-protnlm-function-review.md · genes/DROME/CG5611/CG5611-uniprot.txt

No GO/EC predictions in the reviewed source.

Deep Research

Falcon

(CG5611-deep-research-falcon.md)

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📚 Additional Documentation

Notes

(CG5611-notes.md)

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Bioinformatics Results

(RESULTS.md)

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Protnlm Function Review

(CG5611-protnlm-function-review.md)

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📄 View Raw YAML

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