Search Results
Overview
| Uniprot ID | Q08AH1 |
|---|---|
| Protein Name | Acyl-coenzyme A synthetase ACSM1, mitochondrial |
| Gene Name | ACSM1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 148 | ATILLKAKDILYRLQ |
| 158 | LYRLQLSKAKGIVTI |
| 185 | QCPSLKTKLLVSDHS |
| 204 | LDFRSLVKSASPEHT |
| 237 | TGFPKMAKHSHGLAL |
| 441 | GDPEKTAKVECGDFY |
| 549 | APYKYPRKVEFVSEL |
| 563 | LPKTITGKIERKELR |
Function
Catalyzes the activation of fatty acids by CoA to produce an acyl-CoA, the first step in fatty acid metabolism (PubMed:10434065). Capable of activating medium-chain fatty acids (e.g. butyric (C4) to decanoic (C10) acids), and certain carboxylate-containing xenobiotics, e.g. benzoate (PubMed:10434065). Also catalyzes the activation of lipoate to lipoyl-nucleoside monophosphate (By similarity). Activates lipoate with GTP at a 1000-fold higher rate than with ATP and activates both (R)- and (S)-lipoate to the respective lipoyl-GMP, with a preference for (R)-lipoate (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0072562 | blood microparticle |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005739 | mitochondrion |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0018858 | benzoate-CoA ligase activity |
| Molecular Function | GO:0016405 | CoA-ligase activity |
| Molecular Function | GO:0102391 | decanoate-CoA ligase activity |
| Molecular Function | GO:0015645 | fatty acid ligase activity |
| Molecular Function | GO:0004321 | fatty-acyl-CoA synthase activity |
| Molecular Function | GO:0005525 | GTP binding |
| Molecular Function | GO:0004467 | long-chain fatty acid-CoA ligase activity |
| Molecular Function | GO:0031956 | medium-chain fatty acid-CoA ligase activity |
| Molecular Function | GO:0046872 | metal ion binding |
| Biological Process | GO:0006637 | acyl-CoA metabolic process |
| Biological Process | GO:0018874 | benzoate metabolic process |
| Biological Process | GO:0019605 | butyrate metabolic process |
| Biological Process | GO:0042632 | cholesterol homeostasis |
| Biological Process | GO:0015980 | energy derivation by oxidation of organic compounds |
| Biological Process | GO:0006633 | fatty acid biosynthetic process |
| Biological Process | GO:0019395 | fatty acid oxidation |
| Biological Process | GO:0006805 | xenobiotic metabolic process |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.