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IPR005810 is a Succinyl-CoA ligase, alpha subunit.
<p>This entry describes succinyl-CoA synthetase alpha subunits, but does not discriminate between GTP-specific and ATP-specific reactions. ATP citrate lyases appear to form an outgroup, and are not included in this entry.</p> <p>There are four different enzymes that share a similar catalytic mechanism which involves the phosphorylation by ATP (or GTP) of a specific histidine residue in the active site. These enzymes are:</p> <ul><li>ATP citrate-lyase ([ec:4.1.3.8]) [[cite:PUB00001411]], the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues, catalyses the formation of acetyl-CoA and oxaloacetate from citrate and CoA with the concomitant hydrolysis of ATP to ADP and phosphate. ATP-citrate lyase is a tetramer of identical subunits.</li> <li>Succinyl-CoA ligase (GDP-forming) ([ec:6.2.1.4]) [[cite:PUB00005004]] is a mitochondrial enzyme that catalyses the substrate level phosphorylation step of the tricarboxylic acid cycle: the formation of succinyl-CoA from succinate with a concomitant hydrolysis of GTP to GDP and phosphate. This enzyme is a dimer composed of an alpha and a beta subunits.</li> <li>Succinyl-CoA ligase (ADP-forming) ([ec:6.2.1.5]) [[cite:PUB00000280]] is a bacterial enzyme that during aerobic metabolism functions in the citric acid cycle, coupling the hydrolysis of succinyl-CoA to the synthesis of ATP. It can also function in the other direction for anabolic purposes. This enzyme is a tetramer composed of two alpha and two beta subunits.</li> <li>Malate-CoA ligase ([ec:6.2.1.9]) (malyl-CoA synthetase) [[cite:PUB00002257]], is a bacterial enzyme that forms malyl-CoA from malate and CoA with the concomitant hydrolysis of ATP to ADP and phosphate. Malate-CoA ligase is composed of two different subunits.</li></ul>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Catalytic activity | Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: probable succinyl-CoA ligase [ADP]-forming] gi|502173227|ref|XP_004515280.1| | 21 | ||
| – | Succinate--CoA ligase [ADP]-forming] subunit alpha; TAIR: AT5G23250.1 Succinyl-CoA ligase, alpha subunit; Swiss-Prot: sp|Q8GTQ9|SUCA1_SOLLC Succinate--CoA ligase [ADP]-forming] subunit alpha-1, mitochondrial; TrEMBL-Plants: tr|V7C6K2|V7C6K2_PHAVU Uncharacterized protein; Found in the gene: LotjaGi2g1v0179800 | 22 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| TIGR01019 | TIGRFAM | 1 | 50.00 |