BRENDA - Enzyme Database
show all sequences of 2.5.1.147

Mycobacterium smegmatis mc2 155 fbiC and MSMEG_2392 are involved in triphenylmethane dye decolorization and coenzyme F420 biosynthesis

Guerra-Lopez, D.; Daniels, L.; Rawat, M.; Microbiology 153, 2724-2732 (2007)
No PubMed abstract available

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
Mycolicibacterium smegmatis
the reaction is catalzed by the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
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
Mycolicibacterium smegmatis mc2 155
the reaction is catalzed by the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Mycolicibacterium smegmatis
A0R2I4
-
-
Mycolicibacterium smegmatis mc2 155
A0R2I4
-
-
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
the reaction is catalzed by the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
748607
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
the reaction is catalzed by the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
748607
Mycolicibacterium smegmatis mc2 155
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
-
-
-
?
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine
Mycolicibacterium smegmatis
the reaction is catalzed by the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
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
Mycolicibacterium smegmatis mc2 155
the reaction is catalzed by the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
-
-
?
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
the reaction is catalzed by the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
748607
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
the reaction is catalzed by the bifunctional FO synthase (EC 2.5.1.147/EC 4.3.1.32)
748607
Mycolicibacterium smegmatis mc2 155
5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5'-deoxyadenosine
-
-
-
?
General Information
General Information
Commentary
Organism
metabolism
the enzyme is involved in biosynthesis cofactor coenzyme F420
Mycolicibacterium smegmatis
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme is involved in biosynthesis cofactor coenzyme F420
Mycolicibacterium smegmatis
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
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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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