Recombinant Acidovorax ebreus Succinyl-CoA ligase [ADP-forming] subunit beta (sucC)

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Description

Enzymatic Role and Metabolic Context

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) .

Key Catalytic Features:

PropertyDescription
ReactionSuccinyl-CoA + ADP + Pi ↔ Succinate + ATP + CoA
Cofactor DependencyMg²⁺ or Mn²⁺
Subcellular LocalizationMitochondrial matrix (eukaryotes) or cytosol (prokaryotes)
Structural DomainsATP-grasp domain, conserved nucleotide-binding motifs

Genomic and Functional Traits in Acidovorax Species

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) .

Functional Enrichment in Acidovorax spp.:

CategoryPathogens (Enriched Pfams)Commensals (Enriched Pfams)
EffectorsHrpB (T3SS), pectate lyasesType II secretion systems
Hydrolytic EnzymesChitinases, cellulasesAromatic compound degradation enzymes
MotilityLimitedFlagellar assembly, chemotaxis regulators

Biotechnological and Pathogenic Implications

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 .

Research Gaps and Future Directions

Direct characterization of A. ebreus sucC remains absent in current literature. Priorities include:

  • Heterologous Expression: Kinetic assays to compare ATP/GTP specificity with other SCS isoforms.

  • Succinylome Profiling: Identify succinylation targets in A. ebreus under metabolic stress.

  • Pathogenicity Studies: Assess sucC’s role in biofilm formation or host interaction, as seen in A. citrulli .

Product Specs

Form
Lyophilized powder. We will preferentially ship the format we have in stock. If you have special format requirements, please note them when ordering, and we will fulfill your request.
Lead Time
Delivery times vary by purchase method and location. Consult your local distributor for specific delivery times. All proteins are shipped with standard blue ice packs. For dry ice shipping, please contact us in advance; additional charges apply.
Notes
Avoid repeated freezing and thawing. Working aliquots can be stored at 4°C for up to one week.
Reconstitution
Briefly centrifuge the vial before opening to collect contents at the bottom. Reconstitute the protein in sterile deionized water to a concentration of 0.1-1.0 mg/mL. We recommend adding 5-50% glycerol (final concentration) and aliquoting for long-term storage at -20°C/-80°C. Our default final glycerol concentration is 50%.
Shelf Life
Shelf life depends on several factors: storage conditions, buffer components, storage temperature, and protein stability. Generally, the liquid form is stable for 6 months at -20°C/-80°C, while the lyophilized form is stable for 12 months at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon arrival. Aliquot for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
The tag type will be determined during production. If you require a specific tag, please inform us, and we will prioritize its development.
Synonyms
sucC; Dtpsy_3392; Succinate--CoA ligase [ADP-forming] subunit beta; EC 6.2.1.5; Succinyl-CoA synthetase subunit beta; SCS-beta
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-386
Protein Length
full length protein
Purity
>85% (SDS-PAGE)
Species
Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY))
Target Names
sucC
Target Protein Sequence
MKIHEYQGKE ILRSFGVPVP RGIPAFTVQE AVEAAQKLGG PVWVVKAQIH AGGRGKGGGV KVAKTIDDVK ARASEILGMQ LVTHQTGPEG QKVRRLYIED GADIKNELYV SLVTDRGTQK VALIASSEGG MDIEEVAHST PEKIITEMID PLTGITPEQS KKVAAAIGLT GASVDQAVDL FAKLYKCYMD TDASLVEINP LNCDSKGNLM ALDAKFNFDA NALFRHPEIV ALRDLDEEDP AEVEASKFDL AYISLDGNIG CLVNGAGLAM ATMDTIKLFG GEPANFLDVG GGATPEKVTE AFKIMLKNPK VKGILVNIFG GIMKCDTIAT GVITACKAVN LQVPLVVRMK GTNEELGKKM LAESGLPIIS ADTMAEAATK IVEAVR
Uniprot No.

Target Background

Function
Succinyl-CoA synthetase participates in the citric acid cycle (TCA), coupling succinyl-CoA hydrolysis to ATP or GTP synthesis. This is the only substrate-level phosphorylation step in the TCA cycle. The beta subunit determines nucleotide specificity and binds succinate, while the alpha subunit binds coenzyme A and phosphate.
Database Links
Protein Families
Succinate/malate CoA ligase beta subunit family

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