Information on EC 2.1.1.308 - 2-hydroxyethylphosphonate methyltransferase

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The expected taxonomic range for this enzyme is: Streptomyces

EC NUMBER
COMMENTARY hide
2.1.1.308
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RECOMMENDED NAME
GeneOntology No.
2-hydroxyethylphosphonate methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + methylcob(III)alamin + 2-hydroxyethylphosphonate = 5'-deoxyadenosine + L-methionine + cob(III)alamin + (2S)-2-hydroxypropylphosphonate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
fosfomycin biosynthesis
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Phosphonate and phosphinate metabolism
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:methylcob(III)alamin:2-hydroxyethylphosphonate methyltransferase
Requires cobalamin. The enzyme, isolated from the bacterium Streptomyces wedmorensis, is a member of the 'AdoMet radical' (radical SAM) family. Involved in fosfomycin biosynthesis.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 144-91
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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the enzyme is involved in the biosynthesis of the broad-spectrum antibiotic fosfomycin
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2-hydroxyethyl)phosphonate + S-adenosyl-L-methionine + methylcobalamin
(S)-2-hydroxypropylphosphonate + L-methionine + 5'-deoxyadenosine + cob(II)alamin
show the reaction diagram
S-adenosyl-L-methionine + methylcob(III)alamin + 2-hydroxyethylphosphonate
5'-deoxyadenosine + L-methionine + cob(III)alamin + (2S)-2-hydroxypropylphosphonate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2-hydroxyethyl)phosphonate + S-adenosyl-L-methionine + methylcobalamin
(S)-2-hydroxypropylphosphonate + L-methionine + 5'-deoxyadenosine + cob(II)alamin
show the reaction diagram
S-adenosyl-L-methionine + methylcob(III)alamin + 2-hydroxyethylphosphonate
5'-deoxyadenosine + L-methionine + cob(III)alamin + (2S)-2-hydroxypropylphosphonate
show the reaction diagram
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the enzyme is involved in the biosynthesis of the broad-spectrum antibiotic fosfomycin
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
methylcobalamin
S-adenosyl-L-methionine
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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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
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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
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
multimer
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10 * or 12 * 60400, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning and characterization of a complete fosfomycin biosynthetic cluster from Streptomyces fradiae and heterologous production of fosfomycin in Streptomyces lividans
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C282A
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the mutant enzyme is not able to produce the catalytic [4Fe-4S]+1 cluster
C282A/C286A/C289A
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the triple-variant is very unstable and precipitated during purification and subsequent manipulation for experiments. It completely lacks the [4Fe-4S]+1 cluster
C286A
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the mutant enzyme is not able to produce the catalytic [4Fe-4S]+1 cluster
C289A
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the mutant enzyme is not able to produce the catalytic [4Fe-4S]+1 cluster
additional information