FadD1 (PA3299) is a long-chain fatty acid--CoA ligase (acyl-CoA synthetase) of Pseudomonas aeruginosa that activates exogenous fatty acids as acyl-CoA thioesters, in an ATP-dependent two-step reaction through an acyl-adenylate, at the entry to beta-oxidation. Purified FadD1 prefers long-chain substrates (oleate and palmitate), whereas its genetically linked paralog FadD2 (PA3300) prefers shorter chains. fadD1 mutants grow poorly on fatty acids, especially oleate, and on phosphatidylcholine, a main lipid of lung surfactant, and both fadD genes complement an E. coli fadD mutant. FadD1 is one of several FadD homologs that together let the bacterium use host lipids as nutrients during lung infection.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004467 long-chain fatty acid-CoA ligase activity | IEA GO_REF:0000003 | ACCEPT | Summary: EC 6.2.1.3 mapping. Reason: Core MF, borne out experimentally: purified FadD1 couples CoA to fatty acids with the highest efficiency for C14 to C18 chains. Supporting Evidence: PMID:21042406 FadD1 of P. aeruginosa coupled CoASH to LCFA better than to SCFA or MCFA |
| GO:0006631 fatty acid metabolic process | IBA GO_REF:0000033 | TOO GENERAL | Summary: IBA from the PTN001534887 IBD, seeded by fadD1 itself (PseudoCAP IDA; expected, not circular) and E. coli FadD (P69451; IMP). Reason: True but entailed: GO:0042758 long-chain fatty acid catabolic process, accepted in this review, is_a GO:0006631. The IBD stands on E. coli FadD without this seed, and the generic term suits a node of FadD-type acyl-CoA synthetases. Supporting Evidence: PMID:21042406 fadD1 was found to be important for the metabolism of all FAs, particularly the unsaturated LCFA oleate |
| GO:0006631 fatty acid metabolic process | IDA PMID:21042406 Multiple FadD acyl-CoA synthetases contribute to differentia... | TOO GENERAL | Summary: PseudoCAP IDA; seed of the PTN001534887 IBD. Purified-enzyme kinetics and mutant growth on fatty acids. Seed verdict SOUND. Reason: Correct, but GO:0042758 long-chain fatty acid catabolic process, from the same paper and accepted in this review, is_a GO:0006631. Supporting Evidence: PMID:21042406 FadD1 of P. aeruginosa coupled CoASH to LCFA better than to SCFA or MCFA PMID:21042406 fadD1 was found to be important for the metabolism of all FAs, particularly the unsaturated LCFA oleate |
| GO:0016020 membrane | IEA GO_REF:0000044 | UNDECIDED | Summary: UniProt subcellular location (peripheral membrane protein), itself from an ARBA rule. Reason: E. coli FadD associates peripherally with the inner membrane, and the paper's pathway model places FadD there by analogy, but no location data exist for FadD1. The term can be neither refined nor confirmed without fractionation. Supporting Evidence: PMID:21042406 FA may be transported through the inner membrane via an unknown mechanism coupled to a single peripheral membrane FadD protein |
| GO:0016405 CoA-ligase activity | IBA GO_REF:0000033 | TOO GENERAL | Summary: IBA from the PTN008119558 IBD (E. coli FadD and two M. tuberculosis FadD seeds). Reason: GO:0004467 long-chain fatty acid-CoA ligase activity, accepted in this review, is_a GO:0016405. Supporting Evidence: PMID:21042406 FadD1 of P. aeruginosa coupled CoASH to LCFA better than to SCFA or MCFA |
| GO:0016878 acid-thiol ligase activity | IEA GO_REF:0000117 | TOO GENERAL | Summary: ARBA prediction. Reason: GO:0004467 long-chain fatty acid-CoA ligase activity, accepted in this review, is_a GO:0016878. Supporting Evidence: PMID:21042406 FadD1 of P. aeruginosa coupled CoASH to LCFA better than to SCFA or MCFA |
| GO:0042758 long-chain fatty acid catabolic process | IDA PMID:21042406 Multiple FadD acyl-CoA synthetases contribute to differentia... | ACCEPT | Summary: PseudoCAP IDA. Purified FadD1 activates long-chain fatty acids, and fadD1 mutants grow poorly on them (complemented). Reason: FadD1 performs the activating step of long-chain fatty acid degradation, so it participates in the process; core. Supporting Evidence: PMID:21042406 FadD1 of P. aeruginosa coupled CoASH to LCFA better than to SCFA or MCFA PMID:21042406 fadD1 was found to be important for the metabolism of all FAs, particularly the unsaturated LCFA oleate |
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