Search Results
Overview
| Uniprot ID | Q96I99 |
|---|---|
| Protein Name | Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial |
| Gene Name | SUCLG2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 101 | GVFNSGLKGGVHLTK |
| 108 | KGGVHLTKDPNVVGQ |
| 118 | NVVGQLAKQMIGYNL |
| 128 | IGYNLATKQTPKEGV |
| 132 | LATKQTPKEGVKVNK |
| 139 | KEGVKVNKVMVAEAL |
| 200 | IDIFEGIKDSQAQRM |
| 291 | PIENEAAKYDLKYIG |
| 47 | LQEYQSKKLMSDNGV |
| 73 | NEALEAAKRLNAKEI |
| 78 | AAKRLNAKEIVLKAQ |
| 83 | NAKEIVLKAQILAGG |
| 93 | ILAGGRGKGVFNSGL |
Function
GTP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of GTP and thus represents the only step of substrate-level phosphorylation in the TCA (PubMed:40108300). The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit (By similarity). Also able to act as a GTP-specific itaconyl- and malyl-CoA synthetase (PubMed:40108300)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0042709 | succinate-CoA ligase complex |
| Cellular Component | GO:0045244 | succinate-CoA ligase complex (GDP-forming) |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0019003 | GDP binding |
| Molecular Function | GO:0005525 | GTP binding |
| Molecular Function | GO:0000287 | magnesium ion binding |
| Molecular Function | GO:0044877 | protein-containing complex binding |
| Molecular Function | GO:0004776 | succinate-CoA ligase (GDP-forming) activity |
| Biological Process | GO:0006105 | succinate metabolic process |
| Biological Process | GO:1901289 | succinyl-CoA catabolic process |
| Biological Process | GO:0006104 | succinyl-CoA metabolic process |
| Biological Process | GO:0006099 | tricarboxylic acid cycle |
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.
[3] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.