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Literature summary extracted from

  • Allen, K.D.; Wang, S.C.
    Initial characterization of Fom3 from Streptomyces wedmorensis: The methyltransferase in fosfomycin biosynthesis (2014), Arch. Biochem. Biophys., 543, 67-73.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.308 overexpression in Escherichia coli Rosetta 2 (DE3) pLysS cells as a hexahistidine-tagged protein. The recombinant proteins are found exclusively in inclusion bodies. After refolding and concentration, the protein is reconstituted with additional iron and sulfide to maximize cluster formation Streptomyces wedmorensis

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.308 C282A the mutant enzyme is not able to produce the catalytic [4Fe-4S]+1 cluster Streptomyces wedmorensis
2.1.1.308 C282A/C286A/C289A the triple-variant is very unstable and precipitated during purification and subsequent manipulation for experiments. It completely lacks the [4Fe-4S]+1 cluster Streptomyces wedmorensis
2.1.1.308 C286A the mutant enzyme is not able to produce the catalytic [4Fe-4S]+1 cluster Streptomyces wedmorensis
2.1.1.308 C289A the mutant enzyme is not able to produce the catalytic [4Fe-4S]+1 cluster Streptomyces wedmorensis
2.1.1.308 additional information site-directed mutagenesis of the cysteine residues in the radical SAM CxxxCxxC motif indicates that each residue is essential for functional cluster formation Streptomyces wedmorensis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.308 [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 Streptomyces wedmorensis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.308 60400
-
 10 * or 12 * 60400, SDS-PAGE Streptomyces wedmorensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.308 S-adenosyl-L-methionine + methylcob(III)alamin + 2-hydroxyethylphosphonate Streptomyces wedmorensis the enzyme is involved in the biosynthesis of the broad-spectrum antibiotic fosfomycin 5'-deoxyadenosine + L-methionine + cob(III)alamin + (2S)-2-hydroxypropylphosphonate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.308 Streptomyces wedmorensis Q56184
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.308
-
 Streptomyces wedmorensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.308 S-adenosyl-L-methionine + methylcob(III)alamin + 2-hydroxyethylphosphonate
-
 Streptomyces wedmorensis 5'-deoxyadenosine + L-methionine + cob(III)alamin + (2S)-2-hydroxypropylphosphonate
-
 ?
2.1.1.308 S-adenosyl-L-methionine + methylcob(III)alamin + 2-hydroxyethylphosphonate the enzyme is involved in the biosynthesis of the broad-spectrum antibiotic fosfomycin Streptomyces wedmorensis 5'-deoxyadenosine + L-methionine + cob(III)alamin + (2S)-2-hydroxypropylphosphonate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.308 multimer 10 * or 12 * 60400, SDS-PAGE Streptomyces wedmorensis

Synonyms

EC Number Synonyms Comment Organism
2.1.1.308 fom3
-
 Streptomyces wedmorensis

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.308 Cobalamin
-
 Streptomyces wedmorensis

General Information

EC Number General Information Comment Organism
2.1.1.308 metabolism the enzyme is involved in the biosynthesis of the broad-spectrum antibiotic fosfomycin Streptomyces wedmorensis