Protein Domain : Succinyl-CoA ligase, alpha subunit IPR005810

Type	Family
Description	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 areATP citrate-lyase ( ) [ ], the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues, catalyzes 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.Succinyl-CoA ligase (GDP-forming) ( ) [ ] is a mitochondrial enzyme that catalyzes 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.Succinyl-CoA ligase (ADP-forming) ( ) [ ] 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.Malate-CoA ligase ( ) (malyl-CoA synthetase) [ ], 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.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.
Short Name	CoA_lig_alpha