6.2.1.44	ATP + 3-(methylthio)propanoate + CoA	-	Ruegeria pomeroyi	AMP + diphosphate + 3-(methylthio)propionyl-CoA	-	?	427363	
6.2.1.44	ATP + 3-(methylthio)propanoate + CoA	-	Candidatus Pelagibacter ubique	AMP + diphosphate + 3-(methylthio)propionyl-CoA	-	?	427363	
6.2.1.44	ATP + 3-(methylthio)propanoate + CoA	-	Ruegeria lacuscaerulensis	AMP + diphosphate + 3-(methylthio)propionyl-CoA	-	?	427363	
6.2.1.44	ATP + 3-(methylthio)propanoate + CoA	-	Pseudomonas aeruginosa	AMP + diphosphate + 3-(methylthio)propionyl-CoA	-	?	427363	
6.2.1.44	ATP + 3-(methylthio)propanoate + CoA	-	Burkholderia thailandensis	AMP + diphosphate + 3-(methylthio)propionyl-CoA	-	?	427363	
6.2.1.44	ATP + 3-(methylthio)propanoate + CoA	degradation 3-(methylthio)propanoate, the first product in 3-(dimethylsulfonio)propanoate degradation. 3-(Dimethylsulfonio)propanoate is an osmolyte of many marine algae and certain plants. The global importance of dimethylsulfoniopropionate lies in its availability as a carbon and sulfur source for marine microorganisms and as a precursor of the gas dimethylsulfide, the oceanic emission of which leads to the formation of cloud condensation nuclei and promotion of solar radiation backscatter. Two competing pathways exist for the bacterial catabolism of 3-(dimethylsulfonio)propanoate, one releasing dimethylsulphide and the other releasing methanethiol	Ruegeria pomeroyi	AMP + diphosphate + 3-(methylthio)propionyl-CoA	-	?	427363	
6.2.1.44	ATP + 3-(methylthio)propanoate + CoA	once released from phytoplankton, marine bacteria degrade dimethylsulfoniopropionate by either the cleavage pathway to form the volatile gas dimethylsulfide or the demethylation pathway, yielding methanethiol, which is readily assimilated or oxidized. The enzyme DmdB, a methylmercaptopropionate-coenzyme A ligase, catalyzes the second step in the demethylation pathway and is a major regulatory point. Two forms of DmdB are present in the marine roseobacter Ruegeria pomeroyi DSS-3, RPO_DmdB1 and RPO_DmdB2	Candidatus Pelagibacter ubique	AMP + diphosphate + 3-(methylthio)propionyl-CoA	-	?	427363	
6.2.1.44	ATP + 3-(methylthio)propanoate + CoA	once released from phytoplankton, marine bacteria degrade dimethylsulfoniopropionate by either the cleavage pathway to form the volatile gas dimethylsulfide or the demethylation pathway, yielding methanethiol, which is readily assimilated or oxidized. The enzyme DmdB, a methylmercaptopropionate-coenzyme A ligase, catalyzes the second step in the demethylation pathway and is a major regulatory point. Two forms of DmdB are present in the marine roseobacter Ruegeria pomeroyi DSS-3, RPO_DmdB1 and RPO_DmdB2	Ruegeria pomeroyi	AMP + diphosphate + 3-(methylthio)propionyl-CoA	-	?	427363	
6.2.1.44	ATP + 3-(methylthio)propanoate + CoA	once released from phytoplankton, marine bacteria degrade dimethylsulfoniopropionate by either the cleavage pathway to form the volatile gas dimethylsulfide or the demethylation pathway, yielding methanethiol, which is readily assimilated or oxidized. The enzyme DmdB, a methylmercaptopropionate-coenzyme A ligase, catalyzes the second step in the demethylation pathway and is a major regulatory point. Two forms of DmdB are present in the marine roseobacter Ruegeria pomeroyi DSS-3, RPO_DmdB1 and RPO_DmdB2	Ruegeria pomeroyi	AMP + diphosphate + 3-methylmercaptopropionyl-CoA	-	?	427364	
6.2.1.44	ATP + 3-methylbutanoate + CoA	activity is 14% of the activity with 3-(methylthio)propanoate	Ruegeria pomeroyi	AMP + diphosphate + 3-methylbutanoyl-CoA	-	?	428220