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Literature summary extracted from

  • Woodyer, R.D.; Li, G.; Zhao, H.; van der Donk, W.A.
    New insight into the mechanism of methyl transfer during the biosynthesis of fosfomycin (2007), Chem. Commun. (Camb. ), 4, 359-361.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.308 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/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.99.B6 phosphonoacetaldehyde + reduced acceptor Streptomyces fradiae fomC is required for production of fosfomycin 2-hydroxyethylphosphonate + acceptor
-
?
2.1.1.308 (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

EC Number Organism UniProt Comment Textmining
1.1.99.B6 Streptomyces fradiae D2SNG2
-
-
2.1.1.308 Streptomyces fradiae D2SNF5
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.1.308 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 iron–sulfur 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 and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.99.B6 phosphonoacetaldehyde + reduced acceptor fomC is required for production of fosfomycin Streptomyces fradiae 2-hydroxyethylphosphonate + acceptor
-
?
2.1.1.308 (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
-
?
2.1.1.308 (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

EC Number Synonyms Comment Organism
1.1.99.B6 FomC
-
Streptomyces fradiae
2.1.1.308 fom3
-
Streptomyces fradiae
2.1.1.308 methyltransferase fom3
-
Streptomyces fradiae

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.308 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
2.1.1.308 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

General Information

EC Number General Information Comment Organism
1.1.99.B6 malfunction complementation of fomC disrupted mutants with 2-hydroxyethylphosphonate Streptomyces fradiae