fadE encodes an FAD-dependent acyl-CoA dehydrogenase that oxidizes medium- and long-chain fatty acyl-CoA substrates to trans-2-enoyl-CoA while reducing electron-transfer flavoprotein, initiating each turn of the fatty acid beta-oxidation spiral.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003995 acyl-CoA dehydrogenase activity | IEA GO_REF:0000120 | MARK AS OVER ANNOTATED | Summary: FadE is an acyl-CoA dehydrogenase, but this term is less informative than the supported medium- and long-chain activities. Reason: Retain the chain-length-specific molecular functions as the core annotations. Supporting Evidence: file:PSEPK/fadE/fadE-uniprot.txt Belongs to the acyl-CoA dehydrogenase family. |
| GO:0004466 long-chain fatty acyl-CoA dehydrogenase activity | IEA GO_REF:0000120 | ACCEPT | Summary: FadE catalyzes electron-transfer-flavoprotein-dependent dehydrogenation of long-chain fatty acyl-CoA. Reason: The UniProt reaction and EC assignment directly support this specific activity. Supporting Evidence: file:PSEPK/fadE/fadE-uniprot.txt Reaction=a long-chain 2,3-saturated fatty acyl-CoA + oxidized |
| GO:0005737 cytoplasm | IEA GO_REF:0000118 | UNDECIDED | Summary: Cytoplasmic localization is inferred phylogenetically, while the sequence also has a predicted N-terminal transmembrane segment. Reason: No direct localization evidence is available, and the membrane-associated topology prediction makes an unqualified cytoplasm annotation uncertain. Supporting Evidence: file:PSEPK/fadE/fadE-uniprot.txt TRANSMEM 43..64 |
| GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: This broad oxidoreductase parent is consistent with the reaction but does not identify the acyl-CoA substrate or ETF acceptor. Reason: Retain the specific fatty acyl-CoA dehydrogenase activities. Supporting Evidence: file:PSEPK/fadE/fadE-uniprot.txt Belongs to the acyl-CoA dehydrogenase family. |
| GO:0033539 fatty acid beta-oxidation using acyl-CoA dehydrogenase | IEA GO_REF:0000120 | ACCEPT | Summary: FadE performs the acyl-CoA dehydrogenase step of fatty acid beta-oxidation. Reason: UniProt assigns both the pathway and the defining ETF-dependent reactions. Supporting Evidence: file:PSEPK/fadE/fadE-uniprot.txt PATHWAY: Lipid metabolism; fatty acid beta-oxidation. |
| GO:0050660 flavin adenine dinucleotide binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: FAD is the annotated cofactor for the acyl-CoA dehydrogenase reaction. Reason: Cofactor binding supports catalysis but is not the primary molecular function. Supporting Evidence: file:PSEPK/fadE/fadE-uniprot.txt Name=FAD; Xref=ChEBI:CHEBI:57692; |
| GO:0070991 medium-chain fatty acyl-CoA dehydrogenase activity | IEA GO_REF:0000120 | ACCEPT | Summary: FadE catalyzes electron-transfer-flavoprotein-dependent dehydrogenation of medium-chain fatty acyl-CoA. Reason: The UniProt reaction and EC assignment directly support this specific activity. Supporting Evidence: file:PSEPK/fadE/fadE-uniprot.txt Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + oxidized |
| GO:0006635 fatty acid beta-oxidation | IEA GO_REF:0000041 | ACCEPT | Summary: FadE initiates each turn of the fatty acid beta-oxidation spiral. Reason: The pathway placement and both annotated reactions support this process. Supporting Evidence: file:PSEPK/fadE/fadE-uniprot.txt PATHWAY: Lipid metabolism; fatty acid beta-oxidation. |
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Download this section (compressed HTML)Q: Is FadE membrane-associated in KT2440, and what is the physiological chain-length range of its substrates?
Suggested experts: Pseudomonas fatty acid metabolism experts
Experiment: Measure growth and intracellular acyl-CoA profiles for a fadE deletion and complemented strain across defined medium- and long-chain fatty acids, coupled with membrane fractionation of tagged FadE.
Type: targeted genetics, lipid metabolomics, and subcellular fractionation
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