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Enzyme Nomenclature
Information on EC 1.3.98.7 - [mycofactocin precursor peptide]-tyrosine decarboxylase
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1.3.98.7 [mycofactocin precursor peptide]-tyrosine decarboxylaseIUBMB Comments
This is a bifunctional radical AdoMet (radical SAM) enzyme that catalyses the first two steps in the biosynthesis of the enzyme cofactor mycofactocin. Activity requires the presence of the MftB chaperone. The other activity of the enzyme is EC 4.1.99.26, 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one synthase.
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The expected taxonomic range for this enzyme is: Mycobacteriaceae
Reaction Schemes
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-L-tyrosine
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
mftC
MtfC
mycofactocin maturase
Rv0693
mftC
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-L-tyrosine + S-adenosyl-L-methionine = C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + CO2 + 5'-deoxyadenosine + L-methionine
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-L-tyrosine L-tyrosine-carboxylyase
This is a bifunctional radical AdoMet (radical SAM) enzyme that catalyses the first two steps in the biosynthesis of the enzyme cofactor mycofactocin. Activity requires the presence of the MftB chaperone. The other activity of the enzyme is EC 4.1.99.26, 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one synthase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-L-tyrosine + S-adenosyl-L-methionine
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + CO2 + 5?-deoxyadenosine + L-methionine
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
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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
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-L-tyrosine + S-adenosyl-L-methionine
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + CO2 + 5?-deoxyadenosine + L-methionine
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C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-L-tyrosine + S-adenosyl-L-methionine
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + CO2 + 5?-deoxyadenosine + L-methionine
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additional information
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enzyme additionally catalyzes SAM-dependent C-C bond formation between the Cbeta of the penultimate valine and the Calpha of the former tyrosine, forming a 3-amino-5-[(4-hydroxyphenyl) methyl]-4,4-dimethyl-2-pyrrolidinone moiety, i.e. MftA*, reaction of EC 4.1.99.26
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additional information
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enzyme additionally catalyzes SAM-dependent C-C bond formation between the Cbeta of the penultimate valine and the Calpha of the former tyrosine, forming a 3-amino-5-[(4-hydroxyphenyl) methyl]-4,4-dimethyl-2-pyrrolidinone moiety, i.e. MftA*, reaction of EC 4.1.99.26
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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
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-
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
residues Cys30, 34, and 37 are the radical S-adenosylmethionine ligands
[4Fe-4S]-center
MftC binds a radical S-adenosylmethionine [4Fe-4S] cluster and two auxiliary [4Fe-4S] clusters that are required for MftA modification. Presence of S-adenosylmethionine and MftA affects the environments of the radical S-adenosylmethionine and Aux I cluster whereas the Aux II cluster is unaffected by the substrates. All three cluster are required for cataylsis
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
purified and reconstituted protein contains 10.8 mol of iron and 7.4 mol of sulfide per mol of MftC
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
a MftC deletion mutant is unable to grow in minimal medium containing cholesterol (0.01% [wt/vol]) as the sole carbon source with hot ethanol (1% [vol/vol]) as the solvent (cholesterol and EtOH [cholesterol:EtOH]). There is no significant growth retardation in cholesterol:DMSO. Supplementation of ethanol has no effect on mutant strain growth in propionate (0.5% [wt/vol]) or glycerol (0.2% [vol/vol]) but severely delays mutant strain growth in acetate (0.5% [wt/vol]) in comparison with the growth of the wild-type strain. MftC deletion results in multifold increases in expression of the DosR regulon genes in ethanol-treated strains
physiological function
MtfC is a radical SAM enzyme and oxidatively decarboxylates the C-terminus of the MftA peptide in the presence of the accessory protein MftB. MftC abstracts a hydrogen atom from the beta-carbon of the C-terminal Tyr residue. The resulting radical species is stabilized by the adjacent phenol ring. Decarboxylation occurs either via transfer of the unpaired spin from the radical intermediate to a [4Fe-4S] cluster concomitant with decarboxylation to form the final product. Alternatively, the Calpha-COOH bond can be homolytically cleaved resulting in the formation of a COOH radical species that can either be quenched to formate or CO2
physiological function
radical SAM protein Rv0693 is involved in biosynthesis of cofactor mycofactocin and targets a small peptide for modification
physiological function
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a MftC deletion mutant is unable to grow in minimal medium containing cholesterol (0.01% [wt/vol]) as the sole carbon source with hot ethanol (1% [vol/vol]) as the solvent (cholesterol and EtOH [cholesterol:EtOH]). There is no significant growth retardation in cholesterol:DMSO. Supplementation of ethanol has no effect on mutant strain growth in propionate (0.5% [wt/vol]) or glycerol (0.2% [vol/vol]) but severely delays mutant strain growth in acetate (0.5% [wt/vol]) in comparison with the growth of the wild-type strain. MftC deletion results in multifold increases in expression of the DosR regulon genes in ethanol-treated strains
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physiological function
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MtfC is a radical SAM enzyme and oxidatively decarboxylates the C-terminus of the MftA peptide in the presence of the accessory protein MftB. MftC abstracts a hydrogen atom from the beta-carbon of the C-terminal Tyr residue. The resulting radical species is stabilized by the adjacent phenol ring. Decarboxylation occurs either via transfer of the unpaired spin from the radical intermediate to a [4Fe-4S] cluster concomitant with decarboxylation to form the final product. Alternatively, the Calpha-COOH bond can be homolytically cleaved resulting in the formation of a COOH radical species that can either be quenched to formate or CO2
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physiological function
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radical SAM protein Rv0693 is involved in biosynthesis of cofactor mycofactocin and targets a small peptide for modification
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physiological function
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radical SAM protein Rv0693 is involved in biosynthesis of cofactor mycofactocin and targets a small peptide for modification
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MFTC_MYCUA
Mycobacterium ulcerans (strain Agy99)
369
0
39558
Swiss-Prot
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MFTC_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
392
0
42378
Swiss-Prot
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MFTC_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
391
0
42448
Swiss-Prot
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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**
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**
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein, anaerobically purified using a N-terminal His6-tag. Enzyme is brown in color
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Krishnamoorthy, G.; Kaiser, P.; Lozza, L.; Hahnke, K.; Mollenkopf, H.; Kaufmann, S.
Mycofactocin is associated with ethanol metabolism in mycobacteria
mBio
10
e00190
2019
Mycolicibacterium smegmatis (A0QSB8), Mycolicibacterium smegmatis ATCC 700084 (A0QSB8)
brenda
Bruender, N.A.; Bandarian, V.
The radical S-adenosyl-L-methionine enzyme MftC catalyzes an oxidative decarboxylation of the C-terminus of the MftA peptide
Biochemistry
55
2813-2816
2016
Mycolicibacterium smegmatis (A0QSB8), Mycolicibacterium smegmatis ATCC 700084 (A0QSB8)
-
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
Haft, D.
Bioinformatic evidence for a widely distributed, ribosomally produced electron carrier precursor, its maturation proteins, and its nicotinoprotein redox partners
BMC Genomics
12
21
2011
Mycobacterium tuberculosis (P9WJ79), Mycobacterium tuberculosis H37Rv (P9WJ79)
brenda
Khaliullin, B.; Ayikpoe, R.; Tuttle, M.; Latham, J.
Mechanistic elucidation of the mycofactocin-biosynthetic radical S-adenosylmethionine protein, MftC
J. Biol. Chem.
292
13022-13033
2017
Mycobacterium ulcerans (A0PM49), Mycobacterium ulcerans Agy99 (A0PM49)
brenda
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