6.2.1.1	ADP + acetate + CoA	37% of the activity relative to ATP	Penicillium chrysogenum	AMP + diphosphate + acetyl-CoA	-	?	14	
6.2.1.1	ADP + acetate + CoA	20% of the activity relative to ATP	Bradyrhizobium japonicum	AMP + diphosphate + acetyl-CoA	-	?	14	
6.2.1.1	ADP + phosphate + acetyl-CoA	-	Pyrococcus furiosus	ATP + acetate + CoA	-	?	160	
6.2.1.1	ATP + 2-methylvalerate + CoA	-	Methanothermobacter thermautotrophicus	AMP + diphosphate + 2-methylvaleryl-CoA	-	?	453707	
6.2.1.1	ATP + 3-bromopropanoate + CoA	-	Saccharomyces cerevisiae	AMP + diphosphate + 3-bromopropanoyl-CoA	-	?	141	
6.2.1.1	ATP + 3-chloropropanoate + CoA	-	Saccharomyces cerevisiae	AMP + diphosphate + 3-chloropropanoyl-CoA	-	?	140	
6.2.1.1	ATP + 3-methylvalerate + CoA	mutant enzyme W416G catalyzes the reaction, no activity with wild-type enzyme	Methanothermobacter thermautotrophicus	AMP + diphosphate + 3-methylvaleryl-CoA	-	?	387935	
6.2.1.1	ATP + 4-methylvalerate + CoA	mutant enzyme W416G catalyzes the reaction, no activity with wild-type enzyme	Methanothermobacter thermautotrophicus	AMP + diphosphate + 4-methylvaleryl-CoA	-	?	387938	
6.2.1.1	ATP + acetate + CoA	-	Haloarcula marismortui	AMP + diphosphate + acetyl-CoA	-	r	12	
6.2.1.1	ATP + acetate + CoA	-	Aliivibrio fischeri	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Bacillus subtilis	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Mus musculus	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Escherichia coli	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Rattus norvegicus	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Saccharomyces cerevisiae	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Bos taurus	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Oryctolagus cuniculus	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Euglena gracilis	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Aspergillus nidulans	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Neurospora crassa	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Methanothrix soehngenii	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Cereibacter sphaeroides	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Methanothermobacter thermautotrophicus	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Ovis aries	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Aspergillus niger	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Phycomyces blakesleeanus	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Pinus radiata	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Bradyrhizobium japonicum	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Aedes togoi	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Hordeum vulgare	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Cryptosporidium parvum	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Penicillium chrysogenum	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Spinacia oleracea	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Pisum sativum	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Amaranthus sp.	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Zea mays	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Arabidopsis thaliana	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Pyrococcus furiosus	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Moorella thermoacetica	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Salmonella enterica	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Saccharopolyspora erythraea	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Streptomyces lividans	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Dunaliella tertiolecta	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Pyrobaculum aerophilum	AMP + diphosphate + acetyl-CoA	-	r	12	
6.2.1.1	ATP + acetate + CoA	-	Populus trichocarpa	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Methanosarcina acetivorans	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Homo sapiens	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Pelotomaculum thermopropionicum	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Ignicoccus hospitalis	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Pseudomonas putida	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Rhodotorula diobovata	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	highly specific for ATP	Acetobacter aceti	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	specific for acetate, no activity with other short-chain fatty acids	Oryctolagus cuniculus	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	neither glutathione nor pantetheine can substitute for CoA as acyl acceptor	Bos taurus	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	enzyme is involved in pathway of acetate activation. Cells induce acs transcription, and thus the ability to assimilate acetate, in response to rising cAMP levels, falling oxygen partial pressure, and the flux of carbon through pathways associated with acetate metabolism	Escherichia coli	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	lipogenic enzyme, gene is highly induced by SREBP-1a, SREBP-1c and SREBP-2. The enzyme might also play an important role in basic cellular energy metabolism	Mus musculus	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	no relationship between the enzyme level and the capacity of the plants to incorporate CO2 into labeled fatty acids. Very limited role of the enzyme in the biosynthesis of lipids	Arabidopsis thaliana	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	the enzyme activates acetate so that it can be used for lipid synthesis or for energy generation. The acetyl-CoA synthetase mRNA, and hence the ability of cells to activate acetate, is regulated by sterol regulatory element-binding proteins in parallel with fatty acid synthesis in animal cells	Homo sapiens	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	the bifunctional enzyme carbon monoxide dehydrogenase/acetyl-coenzyme A synthase is a key enzyme in the Wood-Ljungdahl pathway of carbon fixation	Moorella thermoacetica	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	proposed mechanism of the bifunctional enzyme carbon monoxide dehydrogenase/acetyl-coenzyme A synthase	Moorella thermoacetica	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	AceCS2 is reversibly acetylated at Lys642 in the active site of the enzyme. A mammalian sirtuin directly controls the activity of a metabolic enzyme by means of reversible lysine acetylation	Homo sapiens	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	acetate-CoA ligase is a key enzyme for conversion of acetate to acetyl-CoA	Archaeoglobus fulgidus	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	acetate-CoA ligase is a key enzyme for conversion of acetate to acetyl-CoA	Methanothermobacter thermautotrophicus	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	acetyl-CoA synthetase from Pseudomonas putida U is the only acyl-CoA activating enzyme induced by acetate in this bacterium	Pseudomonas putida	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	AF-ACS2 has 2.3fold higher affinity and catalytic efficiency with acetate than with propionate. Enzyme shows a strong preference for ATP versus CTP, GTP, TTP, UTP, ITP or ADP, for which less than 5% activity is observed	Archaeoglobus fulgidus	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	MT-ACS1 is limited to acetate and propionate as acyl substrates. MT-ACS1 has nearly 11fold higher affinity and 14fold higher catalytic efficiency with acetate than with propionate. Enzyme shows a strong preference for ATP versus CTP, GTP, TTP, UTP, ITP or ADP, for which less than 5% activity is observed	Methanothermobacter thermautotrophicus	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	gene acs encoding the enzyme is regulated by quorum sensing, and acs regulation plays a role in symbiosis, overview	Aliivibrio fischeri	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	formation of enzyme-bound acetyl phosphate and enzyme phosphorylation at His257alpha, respectively. The phosphoryl group is transferred from the His257alpha to ADP via transient phosphorylation of a second conserved histidine residue in the beta-subunit, His71beta	Pyrococcus furiosus	AMP + diphosphate + acetyl-CoA	-	ir	12	
6.2.1.1	ATP + acetate + CoA	the ACS reaction is catalyzed at the alpha-subunit A-cluster, an [Fe4S4] cubane bridged to a dinickel [NipNid] subcomponent, overview	Moorella thermoacetica	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	reaction of acetylated ACS with CoA and Fd-II, a step of the catalytic cycle in which the acetylated ACS reacts with CoA to form acetyl-CoA	Moorella thermoacetica	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	activation of acetate in energy metabolism	Methanothrix thermoacetophila	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	activity with propionate is 1% compared to the reactivity with acetate. Butyrate does not serve as a substrate	Methanothrix thermoacetophila	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	important role for motif III (498YTAGD502) in catalysis. The highly conserved Tyr in the first position may play a key role in active-site architecture through interaction with a highly conserved active-site Gln. The invariant Asp in the fifth position plays a critical role in ATP binding and catalysis through interaction with the 2'- and 3'-OH groups of the ribose moiety of ATP	Methanothermobacter thermautotrophicus	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	ATP in form of MgATP2-	Methanothermobacter thermautotrophicus	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Pelotomaculum thermopropionicum JCM10971	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Rhodotorula diobovata MCCC 2A00023	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Ignicoccus hospitalis DSM 18386	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Ignicoccus hospitalis KIN4/IT	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Salmonella enterica G2466	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Saccharopolyspora erythraea NRRL23338	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Saccharomyces cerevisiae LK2G12	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	activation of acetate in energy metabolism	Methanothrix thermoacetophila DSM 6194	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	activity with propionate is 1% compared to the reactivity with acetate. Butyrate does not serve as a substrate	Methanothrix thermoacetophila DSM 6194	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	-	Methanothermobacter thermautotrophicus Z245	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	ATP in form of MgATP2-	Methanothermobacter thermautotrophicus Z245	AMP + diphosphate + acetyl-CoA	-	?	12	
6.2.1.1	ATP + acetate + CoA	enzyme form Acs1p is primarily responsible for acetate activation during gluconeogenic growth. Enzyme form Acs2p is likely to be the major producer of cytosolic acetyl-CoA	Saccharomyces cerevisiae	?	-	?	369316	
6.2.1.1	ATP + acetate + CoA	enzyme plays an important role in the oxidative part of the aceticlastic reaction	Methanothrix soehngenii	?	-	?	369316	
6.2.1.1	ATP + acetate + seleno-CoA	-	Bos taurus	AMP + diphosphate + acetyl-seleno-CoA	-	?	18	
6.2.1.1	ATP + acrylate + CoA	-	Saccharomyces cerevisiae	AMP + diphosphate + acryloyl-CoA	-	?	139	
6.2.1.1	ATP + acrylate + CoA	-	Bos taurus	AMP + diphosphate + acryloyl-CoA	-	?	139	
6.2.1.1	ATP + acrylate + CoA	-	Cereibacter sphaeroides	AMP + diphosphate + acryloyl-CoA	-	?	139	
6.2.1.1	ATP + acrylate + CoA	-	Acetobacter aceti	AMP + diphosphate + acryloyl-CoA	-	?	139	
6.2.1.1	ATP + butyrate + CoA	-	Ovis aries	AMP + diphosphate + butyryl-CoA	-	?	143	
6.2.1.1	ATP + butyrate + CoA	no activity	Acetobacter aceti	AMP + diphosphate + butyryl-CoA	-	?	143	
6.2.1.1	ATP + butyrate + CoA	20% of the activity relative to acetate	Penicillium chrysogenum	AMP + diphosphate + butyryl-CoA	-	?	143	
6.2.1.1	ATP + butyrate + CoA	isobutyrate	Bos taurus	AMP + diphosphate + butyryl-CoA	-	?	143	
6.2.1.1	ATP + butyrate + CoA	25% of the activity with acetate	Pyrobaculum aerophilum	AMP + diphosphate + butyryl-CoA	-	?	143	
6.2.1.1	ATP + butyrate + CoA	26% of the activity with acetyl-CoA	Pseudomonas putida	AMP + diphosphate + butyryl-CoA	-	?	143	
6.2.1.1	ATP + butyrate + CoA	AF-ACS2	Archaeoglobus fulgidus	AMP + diphosphate + butyryl-CoA	-	?	143	
6.2.1.1	ATP + butyrate + CoA	mutant enzymes I312A and W416G catalyzes the reaction, no activity with wild-type enzyme	Methanothermobacter thermautotrophicus	AMP + diphosphate + butyryl-CoA	-	?	143	
6.2.1.1	ATP + butyrate + CoA	mutant enzymes I312A and W416G catalyzes the reaction, no activity with wild-type enzyme	Methanothermobacter thermautotrophicus Z245	AMP + diphosphate + butyryl-CoA	-	?	143	
6.2.1.1	ATP + fluoroacetate + CoA	-	Saccharomyces cerevisiae	AMP + diphosphate + fluoroacetyl-CoA	-	?	20	
6.2.1.1	ATP + fluoroacetate + CoA	-	Bos taurus	AMP + diphosphate + fluoroacetyl-CoA	-	?	20	
6.2.1.1	ATP + formate + CoA	27% of the activity with acetate	Pyrobaculum aerophilum	AMP + diphosphate + formyl-CoA	-	?	379165	
6.2.1.1	ATP + heptanoate + CoA	mutant enzyme W416G catalyzes the reaction, no activity with wild-type enzyme	Methanothermobacter thermautotrophicus	AMP + diphosphate + heptanoyl-CoA	-	?	203	
6.2.1.1	ATP + hexanoate + CoA	mutant enzyme W416G catalyzes the reaction, no activity with wild-type enzyme	Methanothermobacter thermautotrophicus	AMP + diphosphate + hexanoyl-CoA	-	?	202	
6.2.1.1	ATP + hexanoate + CoA	mutant enzyme W416G catalyzes the reaction, no activity with wild-type enzyme	Methanothermobacter thermautotrophicus Z245	AMP + diphosphate + hexanoyl-CoA	-	?	202	
6.2.1.1	ATP + isobutyrate + CoA	28% of the activity with acetate	Pyrobaculum aerophilum	AMP + diphosphate + isobutyryl-CoA	-	?	195	
6.2.1.1	ATP + methacrylic acid + CoA	-	Saccharomyces cerevisiae	AMP + diphosphate + methacryloyl-CoA	-	?	138	
6.2.1.1	ATP + octanoate + CoA	mutant enzyme W416G catalyzes the reaction, no activity with wild-type enzyme	Methanothermobacter thermautotrophicus	AMP + diphosphate + octanoyl-CoA	-	?	204	
6.2.1.1	ATP + pentanoate + CoA	6.7% of the activity relative to acetate	Penicillium chrysogenum	AMP + diphosphate + pentanoyl-CoA	-	?	144	
6.2.1.1	ATP + potassium acetate + CoA	-	Dunaliella tertiolecta	AMP + acetyl-CoA + potassium diphosphate	-	?	443184	
6.2.1.1	ATP + propanoate + CoA	-	Saccharomyces cerevisiae	AMP + diphosphate + propanoyl-CoA	-	?	19	
6.2.1.1	ATP + propanoate + CoA	-	Bos taurus	AMP + diphosphate + propanoyl-CoA	-	?	19	
6.2.1.1	ATP + propanoate + CoA	-	Cereibacter sphaeroides	AMP + diphosphate + propanoyl-CoA	-	?	19	
6.2.1.1	ATP + propanoate + CoA	-	Ovis aries	AMP + diphosphate + propanoyl-CoA	-	?	19	
6.2.1.1	ATP + propanoate + CoA	-	Acetobacter aceti	AMP + diphosphate + propanoyl-CoA	-	?	19	
6.2.1.1	ATP + propanoate + CoA	48% of the activity relative to acetate	Penicillium chrysogenum	AMP + diphosphate + propanoyl-CoA	-	?	19	
6.2.1.1	ATP + propanoate + CoA	very poor activity	Bradyrhizobium japonicum	AMP + diphosphate + propanoyl-CoA	-	?	19	
6.2.1.1	ATP + propanoate + CoA	5% of the activity relative to acetate	Methanothrix soehngenii	AMP + diphosphate + propanoyl-CoA	-	?	19	
6.2.1.1	ATP + propanoate + CoA	118% of the activity with acetate	Pyrobaculum aerophilum	AMP + diphosphate + propanoyl-CoA	-	?	19	
6.2.1.1	ATP + propanoate + CoA	30% of the activity with acetate	Haloarcula marismortui	AMP + diphosphate + propanoyl-CoA	-	?	19	
6.2.1.1	ATP + propionate + CoA	-	Saccharomyces cerevisiae	AMP + diphosphate + propionyl-CoA	-	?	142	
6.2.1.1	ATP + propionate + CoA	-	Methanothermobacter thermautotrophicus	AMP + diphosphate + propionyl-CoA	-	?	142	
6.2.1.1	ATP + propionate + CoA	aerobic taurine dissimilation via acetate kinase and acetate-CoA ligase. Acetate-CoA ligase operates at the end of the pathway	Roseovarius sp.	AMP + diphosphate + propionyl-CoA	-	?	142	
6.2.1.1	ATP + propionate + CoA	nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription. Acs2p is the major acetyl-CoA source for HATs in glucose	Saccharomyces cerevisiae	AMP + diphosphate + propionyl-CoA	-	?	142	
6.2.1.1	ATP + propionate + CoA	55% of the activity with acetyl-CoA	Pseudomonas putida	AMP + diphosphate + propionyl-CoA	-	?	142	
6.2.1.1	ATP + propionate + CoA	AF-ACS2 has 2.3fold higher affinity and catalytic efficiency with acetate than with propionate. Enzyme shows a strong preference for ATP versus CTP, GTP, TTP, UTP, ITP or ADP, for which less than 5% activity is observed	Archaeoglobus fulgidus	AMP + diphosphate + propionyl-CoA	-	?	142	
6.2.1.1	ATP + propionate + CoA	MT-ACS1 is limited to acetate and propionate as acyl substrates. MT-ACS1 has nearly 11fold higher affinity and 14fold higher catalytic efficiency with acetate than with propionate. Enzyme shows a strong preference for ATP versus CTP, GTP, TTP, UTP, ITP or ADP, for which less than 5% activity is observed	Methanothermobacter thermautotrophicus	AMP + diphosphate + propionyl-CoA	-	?	142	
6.2.1.1	ATP + propionate + CoA	aerobic taurine dissimilation via acetate kinase and acetate-CoA ligase. Acetate-CoA ligase operates at the end of the pathway	Roseovarius sp. 217	AMP + diphosphate + propionyl-CoA	-	?	142	
6.2.1.1	ATP + propionate + CoA	-	Methanothermobacter thermautotrophicus Z245	AMP + diphosphate + propionyl-CoA	-	?	142	
6.2.1.1	ATP + sodium acetate + CoA	-	Populus trichocarpa	AMP + acetyl-CoA + sodium diphosphate	-	?	443187	
6.2.1.1	ATP + sodium acetate + CoA	-	Dunaliella tertiolecta	AMP + acetyl-CoA + sodium diphosphate	-	?	443187	
6.2.1.1	ATP + tetrapolyphosphate	-	Saccharomyces cerevisiae	adenosine 5'-pentaphosphate	-	?	146	
6.2.1.1	ATP + tripolyphosphate	-	Saccharomyces cerevisiae	adenosine 5'-tetraphosphate	-	?	145	
6.2.1.1	ATP + valerate + CoA	8% of the activity with acetyl-CoA	Pseudomonas putida	AMP + diphosphate + valeryl-CoA	-	?	368966	
6.2.1.1	ATP + valerate + CoA	mutant enzyme W416G catalyzes the reaction, no activity with wild-type enzyme	Methanothermobacter thermautotrophicus	AMP + diphosphate + valeryl-CoA	-	?	368966	
6.2.1.1	CheY + acetyl-CoA + ATP	CheY is the the excitatory response regulator in the chemotaxis system of Escherichia coli, acetyl-CoA synthetase-catalyzed transfer of acetyl groups from acetate to CheY and autocatalyzed transfer from AcCoA, mechanism, overview	Escherichia coli	acetyl-CheY + CoA + AMP + diphosphate	-	?	398836	
6.2.1.1	CTP + acetate + CoA	-	Penicillium chrysogenum	CMP + diphosphate + acetyl-CoA	-	?	16	
6.2.1.1	dATP + acetate + CoA	-	Mus musculus	dAMP + diphosphate + acetyl-CoA	-	?	13	
6.2.1.1	dATP + acetate + CoA	30% of the activity relative to ATP	Bradyrhizobium japonicum	dAMP + diphosphate + acetyl-CoA	-	?	13	
6.2.1.1	dATP + acetate + CoA	70% of the activity relative to ATP	Bos taurus	dAMP + diphosphate + acetyl-CoA	-	?	13	
6.2.1.1	dATP + acetate + CoA	AceCS2 plays a role in the production of energy under ketogenic conditions, such as starvation and diabetes. Acetyl-CoAs produced by AceCS2 are utilized mainly for oxidation	Mus musculus	dAMP + diphosphate + acetyl-CoA	-	?	13	
6.2.1.1	GTP + acetate + CoA	-	Penicillium chrysogenum	GMP + diphosphate + acetyl-CoA	-	?	17	
6.2.1.1	additional information	-	Oryctolagus cuniculus	?	-	?	89	
6.2.1.1	additional information	enzyme catalyzes propanoate-dependent ATP-diphosphate exchange	Pinus radiata	?	-	?	89	
6.2.1.1	additional information	reaction mechanism of ATP-diphosphate exchange is ordered, ATP is the first substrate to react with the enzyme, and some form of diphosphate is the first product released	Pinus radiata	?	-	?	89	
6.2.1.1	additional information	the enzyme can activate many other molecules to acyl-CoA derivatives: hexanoate, 3-hexenoate, heptanoate, octanoate, 3-octenoate, phenylacetate, 2-thiophene acetate, 3-thiophene acetate	Penicillium chrysogenum	?	-	?	89	
6.2.1.1	additional information	3'-dephospho-CoASH analogues with a phosphodiester bond are not capable of accepting acetate	Oryctolagus cuniculus	?	-	?	89	
6.2.1.1	additional information	enzyme catalyzes acetate-dependent ATP-diphosphate exchange	Bos taurus	?	-	?	89	
6.2.1.1	additional information	enzyme catalyzes acetate-dependent ATP-diphosphate exchange	Pinus radiata	?	-	?	89	
6.2.1.1	additional information	may contribute to the adenosine 5'-tetraphosphate synthesis and adenosine 5'-pentaphosphate synthesis during yeast sporulation	Saccharomyces cerevisiae	?	-	?	89	
6.2.1.1	additional information	the enzyme can catalyze the activation to their CoA thioesters of some of the side-chain precursors required in Penicillium chrysogenum and Aspergillus nidulans for the production of several penicillins	Aspergillus nidulans	?	-	?	89	
6.2.1.1	additional information	the enzyme can catalyze the activation to their CoA thioesters of some of the side-chain precursors required in Penicillium chrysogenum and Aspergillus nidulans for the production of several penicillins	Penicillium chrysogenum	?	-	?	89	
6.2.1.1	additional information	acetate thiokinase is not involved in autotrophic CO2 fixation	Methanothermobacter thermautotrophicus	?	-	?	89	
6.2.1.1	additional information	CODH/ACS is a bifunctional enzyme that is responsible for the reduction of CO2 to CO and subsequent assembly of acetyl-CoA, as part of the Wood-Ljungdahl carbon fixation pathway, the enzyme is a key player in the global carbon cycle	Moorella thermoacetica	?	-	?	89	
6.2.1.1	additional information	metabolic connection between acetate utilization and cell density	Aliivibrio fischeri	?	-	?	89	
6.2.1.1	additional information	role of ACS in destroying fermentative intermediates	Arabidopsis thaliana	?	-	?	89	
6.2.1.1	additional information	the acetyltransferase enzyme, AcuA, controls the activity of the acetyl coenzyme A synthetase, AcsA, by acetylating residue Lys549, overview	Bacillus subtilis	?	-	?	89	
6.2.1.1	additional information	bifunctional Ni-Fe-S containing ACS/CODH, although alpha and beta subunits catalyze separate reactions, they interact functionally when CO2 is used as a substrate in the synthesis of acetyl-CoA	Moorella thermoacetica	?	-	?	89	
6.2.1.1	additional information	the enzyme also forms a carbon-nitrogen bond, reaction of EC 6.3.1 acid-ammonia (or amide) ligase, i.e. amide synthase, and EC 6.3.2 acid-amino acid ligase, i.e. peptide synthase, comprising the amino group of the cysteine and the carboxyl group of the acid, overview	Saccharomyces cerevisiae	?	-	?	89	
6.2.1.1	additional information	the enzyme is a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase, Moorella thermoacetica CODH/ACS contains a very long enzyme channel to allow for intermolecular CO transport, mechanism and reaction steps, overview. Structure-function analysis in comparison to monofunctional Acs, overview	Moorella thermoacetica	?	-	?	89	
6.2.1.1	additional information	the enzyme performs arsenolysis, the alpha-subunit alone also catalyzes arsenolysis, overview	Pyrococcus furiosus	?	-	?	89	
6.2.1.1	additional information	activity determination in a coupled assay with myokinase, pyruvate kinase, and lactate dehydrogenase: SeAcs first converts acetate, CoA, and ATP to acetyl-CoA and AMP. Then, myokinase converts AMP to ADP. Pyruvate kinase converts ADP and phosphoenolpyruvate to pyruvate and ATP. Finally, lactate dehydrogenase reduces pyruvate and oxidizes NADH to NAD+	Salmonella enterica	?	-	?	89	
6.2.1.1	additional information	activity determination in a coupled assay with myokinase, pyruvate kinase, and lactate dehydrogenase: SeAcs first converts acetate, CoA, and ATP to acetyl-CoA and AMP. Then, myokinase converts AMP to ADP. Pyruvate kinase converts ADP and phosphoenolpyruvate to pyruvate and ATP. Finally, lactate dehydrogenase reduces pyruvate and oxidizes NADH to NAD+	Salmonella enterica G2466	?	-	?	89	
6.2.1.1	UTP + acetate + CoA	-	Penicillium chrysogenum	UMP + diphosphate + acetyl-CoA	-	?	15