A1RTB8 · SUCC_PYRIL
- ProteinSuccinate--CoA ligase [ADP-forming] subunit beta
- GenesucC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids382 (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-CoAThis reaction proceeds in the backward direction.
- CoA + GTP + succinate = GDP + phosphate + succinyl-CoAThis reaction proceeds in the backward direction.
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 | 45 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 52-54 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GRG | ||||||
Binding site | 94 | ATP (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 99 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 193 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 207 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 260 | substrate; ligand shared with subunit alpha | ||||
Sequence: N | ||||||
Binding site | 317-319 | substrate; ligand shared with subunit alpha | ||||
Sequence: GIT |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | succinate-CoA ligase (ADP-forming) activity | |
Molecular Function | succinate-CoA ligase (GDP-forming) activity | |
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
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Thermoproteales > Thermoproteaceae > Pyrobaculum
Accessions
- Primary accessionA1RTB8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000082182 | 1-382 | Succinate--CoA ligase [ADP-forming] subunit beta | |||
Sequence: MKLHEYEAKELFLRYGVKIPPGKLALTPDEVRKIAEEIGTPVVLKAQVVVAGRGKAGGIKIAQTPEEAYELSKKMFGMNIKGLVVRKLYVTKYVEVEREMYLSLIIDRASRRYLFLASPIGGVDIEEIAKTSPEKIKKVYVDPSIGLRDYHIRSIISWLGFKPGSQQWQQTASVIQAMYRIMVDYDAELVETNPLALSKEGEVIPLDARVIVDDNALFKHPDLEKALEEDPRDITEFEAYAKKIGFHYVELDGDIGIIGNGAGLTMATMDLVYHFGGRPANFLDIGGGASREVVKEAVKVLLNHPRVKVIFVNIFGGITRADEVALGIKDALAEVKEHTKKIVVRIKGTNEEQGKAILSEIGIPLFENAEEAAKKAVELAKI |
Interaction
Subunit
Heterotetramer of two alpha and two beta subunits.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 9-240 | ATP-grasp | ||||
Sequence: KELFLRYGVKIPPGKLALTPDEVRKIAEEIGTPVVLKAQVVVAGRGKAGGIKIAQTPEEAYELSKKMFGMNIKGLVVRKLYVTKYVEVEREMYLSLIIDRASRRYLFLASPIGGVDIEEIAKTSPEKIKKVYVDPSIGLRDYHIRSIISWLGFKPGSQQWQQTASVIQAMYRIMVDYDAELVETNPLALSKEGEVIPLDARVIVDDNALFKHPDLEKALEEDPRDITEFEAY |
Sequence similarities
Belongs to the succinate/malate CoA ligase beta subunit family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length382
- Mass (Da)42,355
- Last updated2007-02-06 v1
- Checksum06E2854D9DBA68B9
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000504 EMBL· GenBank· DDBJ | ABL88200.1 EMBL· GenBank· DDBJ | Genomic DNA |