Search Results
Overview
| Uniprot ID | P05166 |
|---|---|
| Protein Name | Propionyl-CoA carboxylase beta chain, mitochondrial |
| Gene Name | PCCB |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 248 | QEELGGAKTHTTMSG |
| 373 | LDINSSVKGARFVRF |
| 433 | KVTVITRKAYGGAYD |
| 474 | GAVEIIFKGHENVEA |
| 525 | DLDVLASKKVQRPWR |
| 60 | RRIDAQHKRGKLTAR |
| 99 | DFGMAADKNKFPGDS |
Function
This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites (PubMed:15890657, PubMed:6765947). Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (PubMed:15890657, PubMed:6765947). Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA at a much lower rate (PubMed:6765947). Other alternative minor substrates include (2E)-butenoyl-CoA/crotonoyl-CoA (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005739 | mitochondrion |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0004658 | propionyl-CoA carboxylase activity |
| Biological Process | GO:0009081 | branched-chain amino acid metabolic process |
| Biological Process | GO:0006631 | fatty acid metabolic process |
| Biological Process | GO:0019626 | short-chain fatty acid catabolic 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.