SucC encodes the beta subunit of succinyl-CoA synthetase (SCS), an enzyme essential for the tricarboxylic acid (TCA) cycle. SCS catalyzes the reversible conversion of succinyl-CoA to succinate, coupled with ATP or GTP synthesis . In A. ebreus, this enzyme likely operates in tandem with the alpha subunit (sucD) to form a heterodimer, with the beta subunit determining nucleotide specificity (ATP in this case) .
Comparative pan-genome analyses of Acidovorax strains reveal functional divergences between pathogenic and commensal lineages . While A. ebreus is not explicitly studied in the provided data, sucC homologs in related species show:
Pathogenic Strains: Enriched in hydrolytic enzymes (e.g., pectate lyases, chitinases) and virulence factors .
Commensal Strains: Associated with motility genes (flagella, chemotaxis) and degradation of complex organics (e.g., flavonoids) .
| Category | Pathogens (Enriched Pfams) | Commensals (Enriched Pfams) |
|---|---|---|
| Effectors | HrpB (T3SS), pectate lyases | Type II secretion systems |
| Hydrolytic Enzymes | Chitinases, cellulases | Aromatic compound degradation enzymes |
| Motility | Limited | Flagellar assembly, chemotaxis regulators |
In Staphylococcus aureus, sucC mutations increase succinyl-CoA accumulation, perturbing lysine succinylation and reducing β-lactam resistance . Though unstudied in A. ebreus, sucC likely influences similar post-translational modifications, affecting:
Antioxidant Defense: Upregulation of catalase and peroxiredoxins under oxidative stress .
Stress Granule Formation: Cytosolic relocation of sucC homologs (e.g., SUCLA2 in humans) promotes stress granule assembly, enhancing stress tolerance .
Direct characterization of A. ebreus sucC remains absent in current literature. Priorities include:
KEGG: dia:Dtpsy_3392
STRING: 535289.Dtpsy_3392