LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | The pathway of chloromethane utilization, which allows the microorganisms that possess it to grow with chloromethane as the sole carbon and energy source, is believed to be initiated by a corrinoid-dependent methyltransferase system involving methyltransferase I (CmuA) and methyltransferase II (CmuB), which transfer the methyl group of chloromethane onto tetrahydrofolate (H4folate) [ ]. The methyl group of chloromethane is first transferred by the protein CmuA to a corrinoid protein, from where it is transferred to H4folate by CmuB, yielding methyl-H4folate [, ]. Both CmuA and CmuB display sequence similarity to methyltransferases of methanogenic archaea.CmuA is a two-domain methyltransferase/corrinoid-binding protein involved in methyl transfer from chloromethane to a corrin moiety. CmuA shows similarity to known methyltransferases as well as to their cognate corrinoid protein-binding proteins in the N-terminal and C-terminal parts of its sequence, respectively [ ]. Mutation analysis shows that CmuA acts as methyltransferase I []. Mutation analysis shows that CmuA acts as methyltransferase I []. By analogy to similar methyltransferase systems, it is thought that CmuA acts as both the methyltransferase I and the corrinoid-binding protein in the dehalogenation of chloromethane []. Therefore, CmuA catalyses the first step of the chloromethane-degradation pathway, comprising the dehalogenation of chloromethane and the methylation of an associated cobalt corrin moiety. |
| Short Name | CmuA |
