acetate-CoA ligase. This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.

acetyl-CoA synthetase; Provisional

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme). Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.

Propionyl-CoA synthetase (PrpE). EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.

acetate-CoA ligase

ChainA, Acetyl-coenzyme A synthetase [Salmonella enterica subsp. enterica serovar Typhimurium],2P2Q_B Chain B, Acetyl-coenzyme A synthetase [Salmonella enterica subsp. enterica serovar Typhimurium]

ChainA, Acetyl-coenzyme A synthetase [Salmonella enterica subsp. enterica serovar Typhimurium],2P2J_B Chain B, Acetyl-coenzyme A synthetase [Salmonella enterica subsp. enterica serovar Typhimurium]

ChainA, Acetyl-coenzyme A synthetase [Salmonella enterica subsp. enterica serovar Typhimurium],2P2M_B Chain B, Acetyl-coenzyme A synthetase [Salmonella enterica subsp. enterica serovar Typhimurium]

ChainA, Acetyl-coenzyme A synthetase [Salmonella enterica subsp. enterica serovar Typhimurium],2P2F_B Chain B, Acetyl-coenzyme A synthetase [Salmonella enterica subsp. enterica serovar Typhimurium]

Crystalstructure of Salmonella enterica acetyl-CoA synthetase (Acs) in complex with cAMP and Coenzyme A [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],5JRH_B Crystal structure of Salmonella enterica acetyl-CoA synthetase (Acs) in complex with cAMP and Coenzyme A [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]

Acetyl-coenzyme A synthetase OS=Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01) OX=243265 GN=acs PE=3 SV=1

Acetyl-coenzyme A synthetase 1 OS=Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) OX=160488 GN=acsA1 PE=3 SV=1

Acetyl-coenzyme A synthetase OS=Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) OX=223926 GN=acsA PE=3 SV=1

Acetyl-coenzyme A synthetase OS=Vibrio vulnificus (strain YJ016) OX=196600 GN=acsA PE=3 SV=2

Acetyl-coenzyme A synthetase OS=Yersinia pestis OX=632 GN=acs PE=3 SV=2