2.1.1.308: cytidylyl-2-hydroxyethylphosphonate methyltransferase
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For detailed information about cytidylyl-2-hydroxyethylphosphonate methyltransferase, go to the full flat file.
Reaction
2 S-adenosyl-L-methionine + + = + + + +
Synonyms
(S)-2-hydroxyethylphosphonate methylase, 2-hydroxyethylphosphonate methyltransferase, fom3, methyltransferase fom3
ECTree
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Metals Ions
Metals Ions on EC 2.1.1.308 - cytidylyl-2-hydroxyethylphosphonate methyltransferase
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Fe2+
a conserved domain search of the Fom3 sequence shows it has two conserved domains. The N-terminal domain is identified as a B12-like binding domain, whereas the C-terminal domain shows homology to the radical-SAM protein family, containing three conserved Cys residues that serve as ligands to a [4Fe-4S] cluster
[4Fe-4S] cluster
the [4Fe-4S] cluster undergoes a transition between a +2 resting state and a +1 active state. Site-directed mutagenesis of the cysteine residues in the radical SAM CxxxCxxC motif indicates that each residue is essential for functional cluster formation