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
Biosynthesis of antibiotics
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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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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