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IUBMB Comments The enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO), the precursor of the redox cofactor coenzyme F420 EC 4.3.1.32 , 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, is a radical SAM enzyme that uses the 5′-deoxyadenosyl radical to initiate the reaction.
Synonyms
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EC 2.5.1.77
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formerly, part transferred
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cofH
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fbiC
gene name, bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
fbiC
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gene name, bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32). In the actinomycetes, cofG and cofH are fused, encoding a single FbiC polypeptide
FO synthase
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MjCofH
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MSMEG_5126
gene name, bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
MSMEG_5126
gene name, bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
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5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
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MetaCyc
3PG-factor 420 biosynthesis, factor 420 biosynthesis I (archaea), factor 420 biosynthesis II (mycobacteria)
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5-amino-6-(D-ribitylamino)uracil:L-tyrosine, 4-hydroxyphenyl transferase
The enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO), the precursor of the redox cofactor coenzyme F420, which is found in methanogens and in various actinobacteria. FO is also produced by some cyanobacteria and eukaryotes. The enzyme, which forms a complex with EC 4.3.1.32, 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, is a radical SAM enzyme that uses the 5'-deoxyadenosyl radical to initiate the reaction.
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5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
Substrates: the enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO), the precursor of the redox cofactor coenzyme F420
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5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
Substrates: -
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5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
Substrates: -
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5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
Substrates: the enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO), the precursor of the redox cofactor coenzyme F420
?
5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
Substrates: -
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5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
Substrates: the reaction is catalzed by the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
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5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
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Substrates: the reaction is catalzed by the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
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5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
Substrates: the reaction is catalzed by the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
?
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5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
Substrates: the enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO), the precursor of the redox cofactor coenzyme F420
?
5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
Substrates: the enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO), the precursor of the redox cofactor coenzyme F420
?
5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
Substrates: the reaction is catalzed by the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
?
5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
Substrates: the reaction is catalzed by the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
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Fe2+
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after activation with Fe2+, HS-, S-adenosyl-L-methionine and dithionite, activity increases almost 10fold
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Dithionite
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after activation with Fe2+, HS-, S-adenosyl-L-methionine and dithionite, activity increases almost 10fold
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Uniprot
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Uniprot
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SwissProt
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SwissProt
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SwissProt
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Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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malfunction
four independent mutants that can not make F420 or the biosynthesis intermediate FO contain transposons inserted in the Mycobacterium bovis gene fbiC
metabolism
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the enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin, the precursor of the redox cofactor coenzyme F420. In the actinomycetes, cofG and cofH are fused, encoding a single FbiC polypeptide, the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
metabolism
the enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin, the precursor of the redox cofactor coenzyme F420
metabolism
the enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO), the precursor of the redox cofactor coenzyme F420
metabolism
the enzyme is essential for F420 production
metabolism
the enzyme is involved in biosynthesis cofactor coenzyme F420
metabolism
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the enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin, the precursor of the redox cofactor coenzyme F420
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metabolism
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the enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO), the precursor of the redox cofactor coenzyme F420
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metabolism
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the enzyme is involved in biosynthesis cofactor coenzyme F420
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70
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activity is not significantly reduced during incubations at 70°C
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His-tagged FbiC overexpressed in Escherichia coli
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cloning of the fused Mycobacterium smegmatis fbiC gene and heterologous expression of the bifunctional MsFbiC in Escherichia coli
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heterologous expression in Escherichia coli and functional characterization in vitro. MjCofH is expressed as a fusion protein with an N-terminal polyhistidine tag. The His-tagged protein is strongly expressed in Escherichia coli but is slightly more soluble than the untagged protein
heterologous expression in Escherichia coli and functional characterization in vitro. MjCofH is expressed as a fusion protein with an N-terminal polyhistidine tag. The His-tagged protein is strongly expressed in Escherichia coli but is slightly more soluble than the untagged protein
heterologous expression in Escherichia coli and functional characterization in vitro. MjCofH is expressed as a fusion protein with an N-terminal polyhistidine tag. The His-tagged protein is strongly expressed in Escherichia coli but is slightly more soluble than the untagged protein
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Graham, D.E.; Xu, H.; White, R.H.
Identification of the 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase required for coenzyme F(420) biosynthesis
Arch. Microbiol.
180
455-464
2003
Methanocaldococcus jannaschii (Q58826), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58826), Mycolicibacterium smegmatis
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Philmus, B.; Decamps, L.; Berteau, O.; Begley, T.
Biosynthetic versatility and coordinated action of 5'-deoxyadenosyl radicals in deazaflavin biosynthesis
J. Am. Chem. Soc.
137
5406-5413
2015
Methanocaldococcus jannaschii (Q58826), Methanocaldococcus jannaschii DSM 2661 (Q58826)
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Choi, K.P.; Kendrick, N.; Daniels, L.
Demonstration that fbiC is required by Mycobacterium bovis BCG for coenzyme F(420) and FO biosynthesis
J. Bacteriol.
184
2420-2428
2002
Mycobacterium tuberculosis variant bovis (Q7U0G9)
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Guerra-Lopez, D.; Daniels, L.; Rawat, M.
Mycobacterium smegmatis mc2 155 fbiC and MSMEG_2392 are involved in triphenylmethane dye decolorization and coenzyme F420 biosynthesis
Microbiology
153
2724-2732
2007
Mycolicibacterium smegmatis (A0R2I4), Mycolicibacterium smegmatis mc2 155 (A0R2I4)
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