Search Results
Overview
| Uniprot ID | Q8R4N0 |
|---|---|
| Protein Name | Citramalyl-CoA lyase, mitochondrial |
| Gene Name | Clybl |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 154 | DKFSLHLKGRKLEQP |
| 215 | SIGATSNKDTQDILY |
| 226 | DILYARQKVVVTAKA |
| 307 | KEHQQLGKGAFTFRG |
| 55 | YVPGNDEKKIRKIPS |
| 64 | IRKIPSLKVDCAVLD |
| 80 | EDGVAENKKNEARLR |
| 90 | EARLRIAKTLEDFDL |
Function
Mitochondrial enzyme required to detoxify vitamin B12-poisoning metabolites (PubMed:29056341). Acts as a citramalyl-CoA lyase by converting citramalyl-CoA into acetyl-CoA and pyruvate in the C5-dicarboxylate catabolism pathway, a pathway required to detoxify itaconate, a vitamin B12-poisoning metabolite (By similarity). Also acts as a malyl-CoA thioesterase to detoxify malyl-CoA, a side product of citric acid cycle enzymes, which is toxic for the vitamin B12-dependent enzyme MMUT (By similarity). Also acts as a malate synthase in vitro, converting glyoxylate and acetyl-CoA to malate (By similarity). Also acts as a beta-methylmalate synthase in vitro, by mediating conversion of glyoxylate and propionyl-CoA to beta-methylmalate (By similarity). Also has very weak citramalate synthase activity in vitro (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005739 | mitochondrion |
| Molecular Function | GO:0047777 | (S)-citramalyl-CoA lyase activity |
| Molecular Function | GO:0016289 | acyl-CoA hydrolase activity |
| Molecular Function | GO:0000287 | magnesium ion binding |
| Molecular Function | GO:0004474 | malate synthase activity |
| Biological Process | GO:0106121 | positive regulation of cobalamin metabolic process |
| Biological Process | GO:0070207 | protein homotrimerization |
| Biological Process | GO:0106064 | regulation of cobalamin metabolic process |
| Biological Process | GO:0110052 | toxic metabolite repair |
Reference
[1] Chang J, Wu W, Qian P, Lu Z, He X et al.. Multi-omics study on the effect of moderate-intensity exercise on protein lactylation in mouse muscle tissue.. Front Cell Dev Biol 12:1472338. 2024. PMID: 39935788.
[2] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.
[3] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.