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IUBMB Comments The enzyme, isolated from the bacterium Streptomyces wedmorensis , is involved in fosfomycin biosynthesis. The enzyme also is active as EC 5.4.2.9 phosphoenol pyruvate mutase.
The expected taxonomic range for this enzyme is: Streptomyces wedmorensis
Synonyms Fom1, Fom1CyTase, more
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Fom1
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Fom1
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Fom1 contains a cytidylyltransferase domain at its N-terminus
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2-hydroxyethylphosphonate + CTP = cytidine 5'-{[hydroxy(2-hydroxyethyl)phosphonoyl]phosphate} + diphosphate
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MetaCyc
fosfomycin biosynthesis
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CTP:2-hydroxyethylphosphonate cytidylyltransferase
The enzyme, isolated from the bacterium Streptomyces wedmorensis, is involved in fosfomycin biosynthesis. The enzyme also is active as EC 5.4.2.9 phosphoenolpyruvate mutase.
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2-hydroxyethylphosphonate + CTP
cytidine 5'-[[hydroxy(2-hydroxyethyl)phosphonoyl]phosphate] + diphosphate
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Substrates: - Products: -
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2-hydroxyethylphosphonate + CTP
cytidine 5'-[[hydroxy(2-hydroxyethyl)phosphonoyl]phosphate] + diphosphate
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Substrates: - Products: -
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Co2+
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required for activity. 5 mM used in assay conditions
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FOM1_STRWE
435
0
48290
Swiss-Prot
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native enzyme in complex with cytidine 5'-[[hydroxy(2-hydroxyethyl)phosphonoyl]phosphate], hanging drop vapor diffusion method, using 0.1 M HEPES-NaOH (pH 7.5) and 4.5 M NaCl
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Ni2+-affinity column chromatography
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expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL and B834 (DE3) cells
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Cho, S.H.; Kim, S.Y.; Tomita, T.; Shiraishi, T.; Park, J.S.; Sato, S.; Kudo, F.; Eguchi, T.; Funa, N.; Nishiyama, M.; Kuzuyama, T.
Fosfomycin biosynthesis via transient cytidylylation of 2-hydroxyethylphosphonate by the bifunctional Fom1 enzyme
ACS Chem. Biol.
12
2209-2215
2017
Streptomyces wedmorensis
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