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Succinyl-CoA ligase like flavodoxin domain
This domain contains the catalytic domain from Succinyl-CoA ligase alpha subunit and other related enzymes. A conserved histidine is involved in phosphoryl transfer. [1]. 11781092. Two glutamate residues, Glu 208 alpha and Glu 197 beta, are crucial for phosphorylation and dephosphorylation of the active-site histidine residue in succinyl-CoA synthetase. Fraser ME, Joyce MA, Ryan DG, Wolodko WT;. Biochemistry. 2002;41:537-546. (from Pfam)
CoA binding domain
This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases. [1]. 8144675. The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution. Wolodko WT, Fraser ME, James MN, Bridger WA;. J Biol Chem 1994;269:10883-10890. (from Pfam)
CoA-ligase
This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, malate CoA ligase and ATP-citrate lyase. Some members of the family utilise ATP others use GTP. [1]. 8144675. The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution. Wolodko WT, Fraser ME, James MN, Bridger WA;. J Biol Chem 1994;269:10883-10890. (from Pfam)
succinate--CoA ligase subunit alpha
Catalyzes the only substrate-level phosphorylation in the TCA cycle
succinate--CoA ligase [ADP/GDP-forming] subunit alpha binds the substrates coenzyme A and phosphate as part of the heterodimeric enzyme succinyl-CoA synthetase that functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP
This model describes succinyl-CoA synthetase alpha subunits but does not discriminate between GTP-specific and ATP-specific reactions. The model is designated as subfamily rather than equivalog for that reason. ATP citrate lyases appear to form an outgroup.
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