Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
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 | Streptomyces fradiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2-hydroxyethyl)phosphonate + S-adenosyl-L-methionine + methylcobalamin | Streptomyces fradiae | the enzyme is required for fosfomycin production | (S)-2-hydroxypropylphosphonate + L-methionine + 5'-deoxyadenosine + cob(II)alamin | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces fradiae | D2SNF5 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2 S-adenosyl-L-methionine + cytidine 5'-{[hydroxy(2-hydroxyethyl)phosphonoyl]phosphate} + reduced acceptor = S-adenosyl-L-homocysteine + 5'-deoxyadenosine + L-methionine + cytidine 5'-{[hydroxy(2-hydroxypropyl)phosphonoyl]phosphate} + oxidized acceptor | proposed mechanism: one electron is transferred from the reduced ironsulfur cluster to S-adenosyl-L-methionine to form an adenosyl radical and methionine. The adenosyl radical abstracts the pro-R hydrogen atom from C2 of (S)-2-hydroxyethylphosphonate, and the resulting substrate radical reacts with methylcobalamin yielding (S)-2-hydroxypropylphosphonate and cob(II)alamin. The enzyme is then returned to the active state by reduction of the 4Fe4S cluster back to the +1 state and binding of S-adenosyl-L-methionine and methylcobalamin. Alternatively, cob(II)alamin might be reduced to cob(I)alamin and methylated while bound to the enzyme | Streptomyces fradiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2-hydroxyethyl)phosphonate + S-adenosyl-L-methionine + methylcobalamin | the enzyme is required for fosfomycin production | Streptomyces fradiae | (S)-2-hydroxypropylphosphonate + L-methionine + 5'-deoxyadenosine + cob(II)alamin | - |
? | |
(2-hydroxyethyl)phosphonate + S-adenosyl-L-methionine + methylcobalamin | no activity with (R)-2-hydroxyethylphosphonate | Streptomyces fradiae | (S)-2-hydroxypropylphosphonate + L-methionine + 5'-deoxyadenosine + cob(II)alamin | - |
? |
Synonyms | Comment | Organism |
---|---|---|
fom3 | - |
Streptomyces fradiae |
methyltransferase fom3 | - |
Streptomyces fradiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
methylcobalamin | a B12-derived cofactor. A conserved domain search of the Fom3 sequence shows that 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 | Streptomyces fradiae | |
S-adenosyl-L-methionine | 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 | Streptomyces fradiae |