A0A8J2Z7J6 · A0A8J2Z7J6_9PROT
- ProteinSuccinate--CoA ligase [ADP-forming] subunit beta
- GenesucC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids398 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. 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.
Catalytic activity
- ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
- CoA + GTP + succinate = GDP + phosphate + succinyl-CoA
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Pathway
Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 46 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 53-55 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GRG | ||||||
Binding site | 108 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 111 | ATP (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 116 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 208 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 222 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 273 | substrate; ligand shared with subunit alpha | ||||
Sequence: N | ||||||
Binding site | 330-332 | substrate; ligand shared with subunit alpha | ||||
Sequence: GIA |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | succinate-CoA ligase complex | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | succinate-CoA ligase (ADP-forming) activity | |
Biological Process | succinyl-CoA metabolic process | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSuccinate--CoA ligase [ADP-forming] subunit beta
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Acetobacteraceae > Caldovatus
Accessions
- Primary accessionA0A8J2Z7J6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Heterotetramer of two alpha and two beta subunits.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-212 | ATP-grasp fold succinyl-CoA synthetase-type | ||||
Sequence: NIHEYQAKELLRRYGVAVLDGGVATTPEEAQAIARTLPGPVCAVKAQIHAGGRGAGHFADDPSGKGGVRIARSAEEARAHAAAMLGHTLVTKQTGPAGKVVHRVYVEAGCDIARELYLSLLVDRASGRVAIVASAEGGMDIEEVAEKHPERILRVAVDPASGFSPFHARRLAFGLRLAGAQVGVFTAFVSALHRAFVELDCSIIEINPLVV | ||||||
Domain | 271-391 | ATP-citrate synthase/succinyl-CoA ligase C-terminal | ||||
Sequence: MVNGAGLAMATMDIIKLYGSAPANFLDVGGSATRERVTAAFRIITSDPKVRAILVNIFGGIAKCDLIAEGIVAAAKELTLTVPLVVRLEGTNVAQGRRILAESGLKIIPADNLADAAEKVV |
Sequence similarities
Belongs to the succinate/malate CoA ligase beta subunit family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length398
- Mass (Da)42,023
- Last updated2022-05-25 v1
- Checksum42B548FF187E6B8B
Keywords
- Technical term