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ATP-grasp domain-containing protein
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 beta
ADP/GDP-forming succinate--CoA ligase subunit beta provides nucleotide specificity and binds the succinate substrate for the succinate--CoA ligase enzyme, which functions in the citric acid cycle (TCA) by coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP
succinate-CoA ligase subunit beta
This model is designated subfamily because it does not discriminate the ADP-forming enzyme ((EC 6.2.1.5) from the GDP_forming (EC 6.2.1.4) enzyme. The N-terminal half is described by the CoA-ligases HMM (PF00549). The C-terminal half is described by the ATP-grasp HMM (PF02222). This family contains a split seen both in a maximum parsimony tree (which ignores gaps) and in the gap pattern near position 85 of the seed alignment. Eukaryotic and most bacterial sequences are longer and contain a region similar to TXQTXXXG. Sequences from Deinococcus radiodurans, Mycobacterium tuberculosis, Streptomyces coelicolor, and the Archaea are 6 amino acids shorter in that region and contain a motif resembling [KR]G
ADP-forming succinate--CoA ligase subunit beta
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