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C-terminal [mycofactocin precursor peptide MftA]-glycyl-L-valyl-L-tyrosine + S-adenosyl-L-methionine
C-terminal [mycofactocin precursor peptide MftA]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + CO2 + 5'-deoxyadenosine + L-methionine
dehydro coenzyme F420-0 + FMNH2
oxidized coenzyme F420-0 + FMN
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Substrates: -
Products: -
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oxidized coenzyme F420-0 + FMN
dehydro coenzyme F420-0 + FMNH2
additional information
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C-terminal [mycofactocin precursor peptide MftA]-glycyl-L-valyl-L-tyrosine + S-adenosyl-L-methionine
C-terminal [mycofactocin precursor peptide MftA]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + CO2 + 5'-deoxyadenosine + L-methionine
Substrates: -
Products: -
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C-terminal [mycofactocin precursor peptide MftA]-glycyl-L-valyl-L-tyrosine + S-adenosyl-L-methionine
C-terminal [mycofactocin precursor peptide MftA]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + CO2 + 5'-deoxyadenosine + L-methionine
Substrates: -
Products: -
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oxidized coenzyme F420-0 + FMN
dehydro coenzyme F420-0 + FMNH2
Substrates: -
Products: -
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oxidized coenzyme F420-0 + FMN
dehydro coenzyme F420-0 + FMNH2
Substrates: -
Products: -
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additional information
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Substrates: enzyme additionally displays the activity of EC 4.1.99.26, 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one synthase, forming a 3-amino-5-[(4-hydroxyphenyl) methyl]-4,4-dimethyl-2-pyrrolidinone moiety , i.e. MftA*
Products: -
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additional information
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Substrates: enzyme additionally displays the activity of EC 4.1.99.26, 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one synthase, forming a 3-amino-5-[(4-hydroxyphenyl) methyl]-4,4-dimethyl-2-pyrrolidinone moiety , i.e. MftA*
Products: -
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physiological function
both genes fbiA and fbiB are essential for normal coenzyme F420-5,6 production. fbiA and fbiB constitute an operon. Very low levels of fbiB mRNA are produced by the fbiA mutant
physiological function
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F420 biosynthesis in Thermomicrobia proceeds via dehydro F420, which is reduced by a free-standing FMN-dependent nitroreductase (DF420 reductase) that is distantly related to the C-terminal domain of FbiB
physiological function
FbiB produces cofactor F420 with predominantly 5-7 L-glutamate residues in the poly-gamma-glutamate tail, reactions of EC 6.3.2.31 and 6.3.2.34. The N-terminal domain of FbiB is homologous to CofE with an annotated gamma-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Communication between the two domains is critical for full gamma-glutamyl ligase activity
physiological function
guanylyltransferase FbiD accepts phosphoenolpyruvate, leading to the formation of intermediate dehydro-F420-0. The C-terminal domain of FbiB then utilizes FMNH2 to reduce dehydro-F420-0, which produces mature F420 species when combined with the gamma-glutamyl ligase activity of the N-terminal domain. FbiB also catalyzes the activities of EC 6.3.2.31, coenzyme F420-0:L-glutamate ligase, and EC 6.3.2.34, coenzyme F420-1:gamma-L-glutamate ligase. Expression of genes FbiABCD is sufficient to produce F420 in Escherichia coli
physiological function
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both genes fbiA and fbiB are essential for normal coenzyme F420-5,6 production. fbiA and fbiB constitute an operon. Very low levels of fbiB mRNA are produced by the fbiA mutant
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physiological function
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guanylyltransferase FbiD accepts phosphoenolpyruvate, leading to the formation of intermediate dehydro-F420-0. The C-terminal domain of FbiB then utilizes FMNH2 to reduce dehydro-F420-0, which produces mature F420 species when combined with the gamma-glutamyl ligase activity of the N-terminal domain. FbiB also catalyzes the activities of EC 6.3.2.31, coenzyme F420-0:L-glutamate ligase, and EC 6.3.2.34, coenzyme F420-1:gamma-L-glutamate ligase. Expression of genes FbiABCD is sufficient to produce F420 in Escherichia coli
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physiological function
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FbiB produces cofactor F420 with predominantly 5-7 L-glutamate residues in the poly-gamma-glutamate tail, reactions of EC 6.3.2.31 and 6.3.2.34. The N-terminal domain of FbiB is homologous to CofE with an annotated gamma-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Communication between the two domains is critical for full gamma-glutamyl ligase activity
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physiological function
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FbiB produces cofactor F420 with predominantly 5-7 L-glutamate residues in the poly-gamma-glutamate tail, reactions of EC 6.3.2.31 and 6.3.2.34. The N-terminal domain of FbiB is homologous to CofE with an annotated gamma-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Communication between the two domains is critical for full gamma-glutamyl ligase activity
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C269A
auxiliary [4Fe-4S] cluster I mutant, capable of catalyzing the reductive cleavage of SAM to form dAdo but incapable of converting MftA to MftA* or MftA**
C30A/C37A
radical S-adenosylmethionine mutant, can neither cleave SAM nor modify MftA
C310A/C341A
auxiliary [4Fe-4S] cluster II mutant, capable of catalyzing the reductive cleavage of SAM to form dAdo, incapable of converting MftA to MftA* or MftA**
C323A
auxiliary [4Fe-4S] cluster I mutant, capable of catalyzing the reductive cleavage of SAM to form dAdo, incapable of converting MftA to MftA* or MftA**
C269A
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auxiliary [4Fe-4S] cluster I mutant, capable of catalyzing the reductive cleavage of SAM to form dAdo but incapable of converting MftA to MftA* or MftA**
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C30A/C37A
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radical S-adenosylmethionine mutant, can neither cleave SAM nor modify MftA
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C323A
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auxiliary [4Fe-4S] cluster I mutant, capable of catalyzing the reductive cleavage of SAM to form dAdo, incapable of converting MftA to MftA* or MftA**
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additional information
systematical replacement of Cys residues by Ala. The RS KO could neither cleave SAM nor modify MftA, consistent with the successful knockout of the RS cluster. Activity assays for Aux I and Aux II KO's also provided insightful results. Both Aux I and Aux II KO's were capable of catalyzing the reductive cleavage of SAM to form dAdo (Figure 3A), suggesting that the RS cluster remained intact and in an active conformation in the mutated proteins. However, when assayed against MftA, both Aux I and Aux II KO's were incapable of converting MftA to MftA* or MftA**
additional information
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systematical replacement of Cys residues by Ala. The RS KO could neither cleave SAM nor modify MftA, consistent with the successful knockout of the RS cluster. Activity assays for Aux I and Aux II KO's also provided insightful results. Both Aux I and Aux II KO's were capable of catalyzing the reductive cleavage of SAM to form dAdo (Figure 3A), suggesting that the RS cluster remained intact and in an active conformation in the mutated proteins. However, when assayed against MftA, both Aux I and Aux II KO's were incapable of converting MftA to MftA* or MftA**
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Bashiri, G.; Rehan, A.; Sreebhavan, S.; Baker, H.; Baker, E.; Squire, C.
Elongation of the poly-gamma-glutamate tail of F420 requires both domains of the F420 gamma-glutamyl ligase (FbiB) of Mycobacterium tuberculosis
J. Biol. Chem.
291
6882-6894
2016
Mycobacterium tuberculosis (P9WP79), Mycobacterium tuberculosis H37Rv (P9WP79)
brenda
Bashiri, G.; Antoney, J.; Jirgis, E.NM.; Shah, M.V.; Ney, B.; Copp, J.; Stuteley, S.M.; Sreebhavan, S.; Palmer, B.; Middleditch, M.; Tokuriki, N.; Greening, C.; Scott, C.; Baker, E.N.; Jackson, C.J.
A revised biosynthetic pathway for the cofactor F420 in prokaryotes
Nat. Commun.
10
1558
2019
Mycolicibacterium smegmatis (A0QUZ4), Mycolicibacterium smegmatis ATCC 700084 (A0QUZ4)
brenda
Braga, D.; Hasan, M.; Kroeber, T.; Last, D.; Lackner, G.
Redox coenzyme F420 biosynthesis in thermomicrobia involves reduction by stand-alone nitroreductase superfamily enzymes
Appl. Environ. Microbiol.
86
e00457
2020
Thermomicrobium roseum
brenda
Ayikpoe, R.; Ngendahimana, T.; Langton, M.; Bonitatibus, S.; Walker, L.; Eaton, S.; Eaton, G.; Pandelia, M.; Elliott, S.; Latham, J.
Spectroscopic and electrochemical characterization of the mycofactocin biosynthetic protein, MftC, provides insight into its redox flipping mechanism
Biochemistry
58
940-950
2019
Mycobacterium ulcerans (A0PM49), Mycobacterium ulcerans Agy99 (A0PM49)
brenda
Choi, K.; Bair, T.; Bae, Y.; Daniels, L.
Use of transposon Tn5367 mutagenesis and a nitroimidazopyran-based selection system to demonstrate a requirement for fbiA and fbiB in coenzyme F420 biosynthesis by Mycobacterium bovis BCG
J. Bacteriol.
183
7058-7066
2001
Mycobacterium tuberculosis variant bovis (Q7TWV3), Mycobacterium tuberculosis variant bovis ATCC BAA-935 (Q7TWV3)
brenda