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Information on EC 2.7.7.105 - phosphoenolpyruvate guanylyltransferase
for references in articles please use BRENDA:EC2.7.7.105
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.7 Nucleotidyltransferases
2.7.7.105 phosphoenolpyruvate guanylyltransferase
IUBMB Comments
This enzyme is involved in the biosynthesis of coenzyme F420, a redox-active cofactor, in mycobacteria. cf. EC 2.7.7.68, 2-phospho-L-lactate guanylyltransferase and EC 2.7.7.106, 3-phospho-(R)-glycerate guanylyltransferase.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
showSynonyms
rv2983, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cofC
fbiD
guanylyltransferase
MJ0887
Mtb-FbiD
Rv2983
additional information
fbiD
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phosphoenolpyruvate + GTP = enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
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PATHWAY SOURCE
PATHWAYS
MetaCyc
factor 420 biosynthesis II (mycobacteria)
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SYSTEMATIC NAME
IUBMB Comments
GTP:phosphoenolpyruvate guanylyltransferase
This enzyme is involved in the biosynthesis of coenzyme F420, a redox-active cofactor, in mycobacteria. cf. EC 2.7.7.68, 2-phospho-L-lactate guanylyltransferase and EC 2.7.7.106, 3-phospho-(R)-glycerate guanylyltransferase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
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phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
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Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
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Products: -
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phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
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Substrates: -
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phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
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?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
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additional information
?
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Substrates: CofC from Methanocaldococcus jannaschii accepts 2-phospholactate (96.5%, reaction of EC 2.7.7.68), and phosphoenolpyruvate (3.5%)
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additional information
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Substrates: enzyme Mj-CofC can also catalyze the reaction with ATP, albeit to a lesser extent. No activity with 2-phospho-L-lactate. The CofC enzyme is only active in the presence of FbiA, the inferred intermediate enolpyruvyldiphospho-5'-guanosine (EPPG) is expected to be unstable
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additional information
?
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Substrates: CofC from Methanocaldococcus jannaschii accepts 2-phospholactate (96.5%, reaction of EC 2.7.7.68), and phosphoenolpyruvate (3.5%)
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additional information
?
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Substrates: enzyme Mj-CofC can also catalyze the reaction with ATP, albeit to a lesser extent. No activity with 2-phospho-L-lactate. The CofC enzyme is only active in the presence of FbiA, the inferred intermediate enolpyruvyldiphospho-5'-guanosine (EPPG) is expected to be unstable
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additional information
?
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Substrates: enzyme Mj-CofC can also catalyze the reaction with ATP, albeit to a lesser extent. No activity with 2-phospho-L-lactate. The CofC enzyme is only active in the presence of FbiA, the inferred intermediate enolpyruvyldiphospho-5'-guanosine (EPPG) is expected to be unstable
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additional information
?
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Substrates: enzyme Mj-CofC can also catalyze the reaction with ATP, albeit to a lesser extent. No activity with 2-phospho-L-lactate. The CofC enzyme is only active in the presence of FbiA, the inferred intermediate enolpyruvyldiphospho-5'-guanosine (EPPG) is expected to be unstable
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additional information
?
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Substrates: enzyme Mj-CofC can also catalyze the reaction with ATP, albeit to a lesser extent. No activity with 2-phospho-L-lactate. The CofC enzyme is only active in the presence of FbiA, the inferred intermediate enolpyruvyldiphospho-5'-guanosine (EPPG) is expected to be unstable
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additional information
?
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Substrates: enzyme Mj-CofC can also catalyze the reaction with ATP, albeit to a lesser extent. No activity with 2-phospho-L-lactate. The CofC enzyme is only active in the presence of FbiA, the inferred intermediate enolpyruvyldiphospho-5'-guanosine (EPPG) is expected to be unstable
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additional information
?
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Substrates: CofC from Paraburkholderia rhizoxinica accepts 3-phosphoglycerate (72.7%), 2-phospholactate (23.4%), and phosphoenolpyruvate (3.9%)
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additional information
?
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Substrates: enzyme Mtb-FbiD exclusively utilizes GTP to produce dehydro-F420-0. No activity with 2-phospho-L-lactate. The FbiD enzyme is only active in the presence of FbiA, the inferred intermediate enolpyruvyldiphospho-5'-guanosine (EPPG) is expected to be unstable
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additional information
?
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Substrates: enzyme Mtb-FbiD exclusively utilizes GTP to produce dehydro-F420-0. No activity with 2-phospho-L-lactate. The FbiD enzyme is only active in the presence of FbiA, the inferred intermediate enolpyruvyldiphospho-5'-guanosine (EPPG) is expected to be unstable
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additional information
?
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Substrates: enzyme Mtb-FbiD exclusively utilizes GTP to produce dehydro-F420-0. No activity with 2-phospho-L-lactate. The FbiD enzyme is only active in the presence of FbiA, the inferred intermediate enolpyruvyldiphospho-5'-guanosine (EPPG) is expected to be unstable
Products: -
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additional information
?
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Substrates: enzyme Mtb-FbiD exclusively utilizes GTP to produce dehydro-F420-0. No activity with 2-phospho-L-lactate. The FbiD enzyme is only active in the presence of FbiA, the inferred intermediate enolpyruvyldiphospho-5'-guanosine (EPPG) is expected to be unstable
Products: -
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additional information
?
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Substrates: enzyme Mtb-FbiD exclusively utilizes GTP to produce dehydro-F420-0. No activity with 2-phospho-L-lactate. The FbiD enzyme is only active in the presence of FbiA, the inferred intermediate enolpyruvyldiphospho-5'-guanosine (EPPG) is expected to be unstable
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
phosphoenolpyruvate + GTP
enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
Substrates: -
Products: -
Products: -
?
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
analysis of the evolution of the F420 biosynthesis enzymes (CofC, CofD, CofE, CofG and CofH) to understand the origin and distribution of the cofactor, phylogenetic analysis and tree, overview. F420 biosynthesis pathways evolved through bacterial-to-archaeal horizontal gene transfers
evolution
analysis of the evolution of the F420 biosynthesis enzymes (CofC, CofD, CofE, CofG and CofH) to understand the origin and distribution of the cofactor, phylogenetic analysis and tree, overview. F420 biosynthesis pathways evolved through bacterial-to-archaeal horizontal gene transfers
evolution
structure comparisons of bacterial FbiD and archaeal CofC enzymes. Mtb-FbiD adopts the same MobA-like nucleoside triphosphate transferase family protein fold as CofC: central 7-stranded beta-sheet (six parallel strands and one antiparallel), with alpha-helices packed on either side. But Mtb-FbiD lacks the protruding hairpin that is important for dimer formation in CofC
evolution
structure comparisons of bacterial FbiD and archaeal CofC enzymes. Mtb-FbiD adopts the same MobA-like nucleoside triphosphate transferase family protein fold as CofC: central 7-stranded beta-sheet (six parallel strands and one antiparallel), with alpha-helices packed on either side. But Mtb-FbiD lacks the protruding hairpin that is important for dimer formation in CofC
evolution
-
analysis of the evolution of the F420 biosynthesis enzymes (CofC, CofD, CofE, CofG and CofH) to understand the origin and distribution of the cofactor, phylogenetic analysis and tree, overview. F420 biosynthesis pathways evolved through bacterial-to-archaeal horizontal gene transfers
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evolution
-
structure comparisons of bacterial FbiD and archaeal CofC enzymes. Mtb-FbiD adopts the same MobA-like nucleoside triphosphate transferase family protein fold as CofC: central 7-stranded beta-sheet (six parallel strands and one antiparallel), with alpha-helices packed on either side. But Mtb-FbiD lacks the protruding hairpin that is important for dimer formation in CofC
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evolution
-
structure comparisons of bacterial FbiD and archaeal CofC enzymes. Mtb-FbiD adopts the same MobA-like nucleoside triphosphate transferase family protein fold as CofC: central 7-stranded beta-sheet (six parallel strands and one antiparallel), with alpha-helices packed on either side. But Mtb-FbiD lacks the protruding hairpin that is important for dimer formation in CofC
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evolution
-
structure comparisons of bacterial FbiD and archaeal CofC enzymes. Mtb-FbiD adopts the same MobA-like nucleoside triphosphate transferase family protein fold as CofC: central 7-stranded beta-sheet (six parallel strands and one antiparallel), with alpha-helices packed on either side. But Mtb-FbiD lacks the protruding hairpin that is important for dimer formation in CofC
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evolution
-
structure comparisons of bacterial FbiD and archaeal CofC enzymes. Mtb-FbiD adopts the same MobA-like nucleoside triphosphate transferase family protein fold as CofC: central 7-stranded beta-sheet (six parallel strands and one antiparallel), with alpha-helices packed on either side. But Mtb-FbiD lacks the protruding hairpin that is important for dimer formation in CofC
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evolution
-
analysis of the evolution of the F420 biosynthesis enzymes (CofC, CofD, CofE, CofG and CofH) to understand the origin and distribution of the cofactor, phylogenetic analysis and tree, overview. F420 biosynthesis pathways evolved through bacterial-to-archaeal horizontal gene transfers
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evolution
-
analysis of the evolution of the F420 biosynthesis enzymes (CofC, CofD, CofE, CofG and CofH) to understand the origin and distribution of the cofactor, phylogenetic analysis and tree, overview. F420 biosynthesis pathways evolved through bacterial-to-archaeal horizontal gene transfers
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evolution
-
structure comparisons of bacterial FbiD and archaeal CofC enzymes. Mtb-FbiD adopts the same MobA-like nucleoside triphosphate transferase family protein fold as CofC: central 7-stranded beta-sheet (six parallel strands and one antiparallel), with alpha-helices packed on either side. But Mtb-FbiD lacks the protruding hairpin that is important for dimer formation in CofC
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evolution
-
structure comparisons of bacterial FbiD and archaeal CofC enzymes. Mtb-FbiD adopts the same MobA-like nucleoside triphosphate transferase family protein fold as CofC: central 7-stranded beta-sheet (six parallel strands and one antiparallel), with alpha-helices packed on either side. But Mtb-FbiD lacks the protruding hairpin that is important for dimer formation in CofC
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evolution
-
analysis of the evolution of the F420 biosynthesis enzymes (CofC, CofD, CofE, CofG and CofH) to understand the origin and distribution of the cofactor, phylogenetic analysis and tree, overview. F420 biosynthesis pathways evolved through bacterial-to-archaeal horizontal gene transfers
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evolution
-
structure comparisons of bacterial FbiD and archaeal CofC enzymes. Mtb-FbiD adopts the same MobA-like nucleoside triphosphate transferase family protein fold as CofC: central 7-stranded beta-sheet (six parallel strands and one antiparallel), with alpha-helices packed on either side. But Mtb-FbiD lacks the protruding hairpin that is important for dimer formation in CofC
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metabolism
archaeal guanylyltransferase CofC, along with its the bacterial homologue FbiD, accepts ohosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0. The enzyme is involved in the F420-0 biosynthetic pathway, overview. Dehydro-F420-0 is a bona fide metabolic intermediate that can be converted to mature F420 by FbiB in an FMNH2-dependent fashion
metabolism
the guanylyltransferase FbiD, along with its archaeal homologue CofC, accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the 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. The enzyme is involved in the F420-0 biosynthetic pathway, overview. Dehydro-F420-0 is a bona fide metabolic intermediate that can be converted to mature F420 by FbiB in an FMNH2-dependent fashion
metabolism
-
archaeal guanylyltransferase CofC, along with its the bacterial homologue FbiD, accepts ohosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0. The enzyme is involved in the F420-0 biosynthetic pathway, overview. Dehydro-F420-0 is a bona fide metabolic intermediate that can be converted to mature F420 by FbiB in an FMNH2-dependent fashion
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metabolism
-
archaeal guanylyltransferase CofC, along with its the bacterial homologue FbiD, accepts ohosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0. The enzyme is involved in the F420-0 biosynthetic pathway, overview. Dehydro-F420-0 is a bona fide metabolic intermediate that can be converted to mature F420 by FbiB in an FMNH2-dependent fashion
-
metabolism
-
archaeal guanylyltransferase CofC, along with its the bacterial homologue FbiD, accepts ohosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0. The enzyme is involved in the F420-0 biosynthetic pathway, overview. Dehydro-F420-0 is a bona fide metabolic intermediate that can be converted to mature F420 by FbiB in an FMNH2-dependent fashion
-
metabolism
-
archaeal guanylyltransferase CofC, along with its the bacterial homologue FbiD, accepts ohosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0. The enzyme is involved in the F420-0 biosynthetic pathway, overview. Dehydro-F420-0 is a bona fide metabolic intermediate that can be converted to mature F420 by FbiB in an FMNH2-dependent fashion
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metabolism
-
the guanylyltransferase FbiD, along with its archaeal homologue CofC, accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the 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. The enzyme is involved in the F420-0 biosynthetic pathway, overview. Dehydro-F420-0 is a bona fide metabolic intermediate that can be converted to mature F420 by FbiB in an FMNH2-dependent fashion
-
metabolism
-
the guanylyltransferase FbiD, along with its archaeal homologue CofC, accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the 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. The enzyme is involved in the F420-0 biosynthetic pathway, overview. Dehydro-F420-0 is a bona fide metabolic intermediate that can be converted to mature F420 by FbiB in an FMNH2-dependent fashion
-
metabolism
-
archaeal guanylyltransferase CofC, along with its the bacterial homologue FbiD, accepts ohosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0. The enzyme is involved in the F420-0 biosynthetic pathway, overview. Dehydro-F420-0 is a bona fide metabolic intermediate that can be converted to mature F420 by FbiB in an FMNH2-dependent fashion
-
physiological function
guanylyltransferase FbiD accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0. The C-terminal domain of gamma-glutamyl ligase 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. Expression of the FbiABCD cluster is sufficient to produce F420 in Escherichia coli
physiological function
archaeal guanylyltransferase CofC, along with its the bacterial homologue FbiD, accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0
physiological function
the guanylyltransferase FbiD, along with its archaeal homologue CofC, accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0
physiological function
-
archaeal guanylyltransferase CofC, along with its the bacterial homologue FbiD, accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0
-
physiological function
-
archaeal guanylyltransferase CofC, along with its the bacterial homologue FbiD, accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0
-
physiological function
-
archaeal guanylyltransferase CofC, along with its the bacterial homologue FbiD, accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0
-
physiological function
-
archaeal guanylyltransferase CofC, along with its the bacterial homologue FbiD, accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0
-
physiological function
-
the guanylyltransferase FbiD, along with its archaeal homologue CofC, accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0
-
physiological function
-
guanylyltransferase FbiD accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0. The C-terminal domain of gamma-glutamyl ligase 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. Expression of the FbiABCD cluster is sufficient to produce F420 in Escherichia coli
-
physiological function
-
the guanylyltransferase FbiD, along with its archaeal homologue CofC, accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0
-
physiological function
-
archaeal guanylyltransferase CofC, along with its the bacterial homologue FbiD, accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the intermediate dehydro-F420-0
-
additional information
-
docking of dehydro-F420-0 into the FMNH2-bound structure of FbiD. The methylene group of dehydro F420-0 is accommodated by a small hydrophobic pocket mostly comprised of P289 and M372 allowing it to be positioned above the N5 atom of FMNH2, in a plausible Michaelis complex for hydride transfer. The phosphoenolpyruvyl group of dehydro-F420-0 most likely samples conformations within this pocket where it can be reduced
additional information
docking of dehydro-F420-0 into the FMNH2-bound structure of FbiD. The methylene group of dehydro F420-0 is accommodated by a small hydrophobic pocket mostly comprised of P289 and M372 allowing it to be positioned above the N5 atom of FMNH2, in a plausible Michaelis complex for hydride transfer. The phosphoenolpyruvyl group of dehydro-F420-0 most likely samples conformations within this pocket where it can be reduced
additional information
-
docking of dehydro-F420-0 into the FMNH2-bound structure of FbiD. The methylene group of dehydro F420-0 is accommodated by a small hydrophobic pocket mostly comprised of P289 and M372 allowing it to be positioned above the N5 atom of FMNH2, in a plausible Michaelis complex for hydride transfer. The phosphoenolpyruvyl group of dehydro-F420-0 most likely samples conformations within this pocket where it can be reduced
-
additional information
-
docking of dehydro-F420-0 into the FMNH2-bound structure of FbiD. The methylene group of dehydro F420-0 is accommodated by a small hydrophobic pocket mostly comprised of P289 and M372 allowing it to be positioned above the N5 atom of FMNH2, in a plausible Michaelis complex for hydride transfer. The phosphoenolpyruvyl group of dehydro-F420-0 most likely samples conformations within this pocket where it can be reduced
-
Show AA Sequence and Transmembrane Helices (3089 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native structure, to 1.99 A resolution, in complex with phosphoenolpyruvate, to 2.18 A resolution
purified recombinant wild-type and SeMet-labeled enzyme FbiD in apoform and in complex with phosphoenolpyruvate, X-ray diffraction structure determination and analysis at 1.99-2.33 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
expression of the enzyme and by construction of a functional F420 biosynthetic pathway in Escherichia coli, an organism that does not normally produce F420, at levels comparable to some native F420-producing organisms
additional information
-
expression of the enzyme and by construction of a functional F420 biosynthetic pathway in Escherichia coli, an organism that does not normally produce F420, at levels comparable to some native F420-producing organisms
-
additional information
-
expression of the enzyme and by construction of a functional F420 biosynthetic pathway in Escherichia coli, an organism that does not normally produce F420, at levels comparable to some native F420-producing organisms
-
additional information
-
expression of the enzyme and by construction of a functional F420 biosynthetic pathway in Escherichia coli, an organism that does not normally produce F420, at levels comparable to some native F420-producing organisms
-
additional information
-
expression of the enzyme and by construction of a functional F420 biosynthetic pathway in Escherichia coli, an organism that does not normally produce F420, at levels comparable to some native F420-producing organisms
-
additional information
-
expression of the enzyme and by construction of a functional F420 biosynthetic pathway in Escherichia coli, an organism that does not normally produce F420, at levels comparable to some native F420-producing organisms
-
additional information
-
expression of the enzyme and by construction of a functional F420 biosynthetic pathway in Escherichia coli, an organism that does not normally produce F420, at levels comparable to some native F420-producing organisms. Expression of fbiABCD is sufficient to produce F420 in Escherichia coli
additional information
expression of the enzyme and by construction of a functional F420 biosynthetic pathway in Escherichia coli, an organism that does not normally produce F420, at levels comparable to some native F420-producing organisms. Expression of fbiABCD is sufficient to produce F420 in Escherichia coli
additional information
-
expression of the enzyme and by construction of a functional F420 biosynthetic pathway in Escherichia coli, an organism that does not normally produce F420, at levels comparable to some native F420-producing organisms. Expression of fbiABCD is sufficient to produce F420 in Escherichia coli
-
additional information
-
expression of the enzyme and by construction of a functional F420 biosynthetic pathway in Escherichia coli, an organism that does not normally produce F420, at levels comparable to some native F420-producing organisms. Expression of fbiABCD is sufficient to produce F420 in Escherichia coli
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene fbiD, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree
gene fbiD, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree
gene fbiD, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
the 3PG-F420 biosynthetic gene cluster is fully functional in Escherichia coli, enabling convenient production of the cofactor by fermentation
synthesis
-
the 3PG-F420 biosynthetic gene cluster is fully functional in Escherichia coli, enabling convenient production of the cofactor by fermentation
synthesis
-
the 3PG-F420 biosynthetic gene cluster is fully functional in Escherichia coli, enabling convenient production of the cofactor by fermentation
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Braga, D.; Last, D.; Hasan, M.; Guo, H.; Leichnitz, D.; Uzum, Z.; Richter, I.; Schalk, F.; Beemelmanns, C.; Hertweck, C.; Lackner, G.
Metabolic pathway rerouting in Paraburkholderia rhizoxinica evolved long-overlooked derivatives of coenzyme F420
ACS Chem. Biol.
14
2088-2094
2019
Methanocaldococcus jannaschii (Q58297), Methanocaldococcus jannaschii ATCC 43067 (Q58297), Mycetohabitans rhizoxinica
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
Methanocaldococcus jannaschii (Q58297), Methanocaldococcus jannaschii ATCC 43067 (Q58297), Methanocaldococcus jannaschii DSM 2661 (Q58297), Methanocaldococcus jannaschii JAL-1 (Q58297), Methanocaldococcus jannaschii JCM 10045 (Q58297), Methanocaldococcus jannaschii NBRC 100440 (Q58297), Mycobacterium tuberculosis, Mycobacterium tuberculosis (P9WP83), Mycobacterium tuberculosis ATCC 25618, Mycobacterium tuberculosis ATCC 25618 (P9WP83), Mycobacterium tuberculosis H37Rv (P9WP83)
brenda
Ney, B.; Ahmed, F.; Carere, C.; Biswas, A.; Warden, A.; Morales, S.; Pandey, G.; Watt, S.; Oakeshott, J.; Taylor, M.; Stott, M.; Jackson, C.; Greening, C.
The methanogenic redox cofactor F420 is widely synthesized by aerobic soil bacteria
ISME J.
11
125-137
2016
Mycolicibacterium smegmatis (A0QUZ4), Mycolicibacterium smegmatis ATCC 700084 (A0QUZ4), Thermomicrobium roseum (B9L4T8), Thermomicrobium roseum ATCC 27502 (B9L4T8), Thermomicrobium roseum DSM 5159 (B9L4T8), Thermomicrobium roseum P-2 (B9L4T8)
brenda
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Release 2023.1 (January 2023)
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