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show all sequences of 2.5.1.147

Identification of the 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase required for coenzyme F(420) biosynthesis

Graham, D.E.; Xu, H.; White, R.H.; Arch. Microbiol. 180, 455-464 (2003)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
Dithionite
after activation with Fe2+, HS-, S-adenosyl-L-methionine and dithionite, activity increases almost 10fold
Mycolicibacterium smegmatis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
after activation with Fe2+, HS-, S-adenosyl-L-methionine and dithionite, activity increases almost 10fold
Mycolicibacterium smegmatis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
SDS-PAGE
Methanocaldococcus jannaschii
88000
-
SDS-PAGE
Mycolicibacterium smegmatis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanocaldococcus jannaschii
Q58826
-
-
Methanocaldococcus jannaschii DSM 2661
Q58826
-
-
Mycolicibacterium smegmatis
A0A0D6IWS7
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
-
746934
Methanocaldococcus jannaschii
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
the reaction is catalzed by the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
746934
Mycolicibacterium smegmatis
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
-
746934
Methanocaldococcus jannaschii DSM 2661
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
-
-
-
?
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
70
-
activity is not significantly reduced during incubations at 70°C
Mycolicibacterium smegmatis
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
Dithionite
after activation with Fe2+, HS-, S-adenosyl-L-methionine and dithionite, activity increases almost 10fold
Mycolicibacterium smegmatis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
after activation with Fe2+, HS-, S-adenosyl-L-methionine and dithionite, activity increases almost 10fold
Mycolicibacterium smegmatis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
SDS-PAGE
Methanocaldococcus jannaschii
88000
-
SDS-PAGE
Mycolicibacterium smegmatis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
-
746934
Methanocaldococcus jannaschii
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
the reaction is catalzed by the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
746934
Mycolicibacterium smegmatis
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
-
746934
Methanocaldococcus jannaschii DSM 2661
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
-
-
-
?
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
70
-
activity is not significantly reduced during incubations at 70°C
Mycolicibacterium smegmatis
Expression
Organism
Commentary
Expression
Methanocaldococcus jannaschii
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
additional information
Mycolicibacterium smegmatis
cloning of the fused Mycobacterium smegmatis fbiC gene and heterologous expression of the bifunctional MsFbiC in Escherichia coli
additional information
General Information
General Information
Commentary
Organism
metabolism
the enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin, the precursor of the redox cofactor coenzyme F420
Methanocaldococcus jannaschii
metabolism
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)
Mycolicibacterium smegmatis
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin, the precursor of the redox cofactor coenzyme F420
Methanocaldococcus jannaschii
metabolism
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)
Mycolicibacterium smegmatis
Expression (protein specific)
Organism
Commentary
Expression
Methanocaldococcus jannaschii
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
additional information
Mycolicibacterium smegmatis
cloning of the fused Mycobacterium smegmatis fbiC gene and heterologous expression of the bifunctional MsFbiC in Escherichia coli
additional information
Other publictions for EC 2.5.1.147
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
748030
Philmus
Biosynthetic versatility and ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
J. Am. Chem. Soc.
137
5406-5413
2015
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748607
Guerra-Lopez
-
Mycobacterium smegmatis mc2 1 ...
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc2 155
Microbiology
153
2724-2732
2007
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746934
Graham
Identification of the 7,8-did ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661, Mycolicibacterium smegmatis
Arch. Microbiol.
180
455-464
2003
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748075
Choi
Demonstration that fbiC is re ...
Mycobacterium tuberculosis variant bovis
J. Bacteriol.
184
2420-2428
2002
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