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Literature summary for 2.7.7.105 extracted from

  • 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 (2019), Nat. Commun., 10, 1558 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.105

Cloned(Commentary)

Cloned (Comment) Organism
gene cofC, recombinant expression in Escherichia coli Methanocaldococcus jannaschii
gene fbiD, recombinant expression in Escherichia coli Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
native structure, to 1.99 A resolution, in complex with phosphoenolpyruvate, to 2.18 A resolution Mycobacterium tuberculosis
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 Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
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 Methanocaldococcus jannaschii
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 Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phosphoenolpyruvate + GTP Methanocaldococcus jannaschii
-
 enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
 ?
phosphoenolpyruvate + GTP Mycobacterium tuberculosis
-
 enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
 ?
phosphoenolpyruvate + GTP Methanocaldococcus jannaschii NBRC 100440
-
 enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
 ?
phosphoenolpyruvate + GTP Methanocaldococcus jannaschii DSM 2661
-
 enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
 ?
phosphoenolpyruvate + GTP Methanocaldococcus jannaschii ATCC 43067
-
 enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
 ?
phosphoenolpyruvate + GTP Methanocaldococcus jannaschii JAL-1
-
 enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
 ?
phosphoenolpyruvate + GTP Mycobacterium tuberculosis H37Rv
-
 enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
 ?
phosphoenolpyruvate + GTP Mycobacterium tuberculosis ATCC 25618
-
 enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
 ?
phosphoenolpyruvate + GTP Methanocaldococcus jannaschii JCM 10045
-
 enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii Q58297 Methanococcus jannaschii
-
Methanocaldococcus jannaschii ATCC 43067 Q58297 Methanococcus jannaschii
-
Methanocaldococcus jannaschii DSM 2661 Q58297 Methanococcus jannaschii
-
Methanocaldococcus jannaschii JAL-1 Q58297 Methanococcus jannaschii
-
Methanocaldococcus jannaschii JCM 10045 Q58297 Methanococcus jannaschii
-
Methanocaldococcus jannaschii NBRC 100440 Q58297 Methanococcus jannaschii
-
Mycobacterium tuberculosis
-
-
-
Mycobacterium tuberculosis P9WP83
-
-
Mycobacterium tuberculosis ATCC 25618
-
-
-
Mycobacterium tuberculosis ATCC 25618 P9WP83
-
-
Mycobacterium tuberculosis H37Rv P9WP83
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 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 Methanocaldococcus jannaschii ?
-
-
additional information 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 Mycobacterium tuberculosis ?
-
-
additional information 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 Methanocaldococcus jannaschii NBRC 100440 ?
-
-
additional information 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 Methanocaldococcus jannaschii DSM 2661 ?
-
-
additional information 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 Methanocaldococcus jannaschii ATCC 43067 ?
-
-
additional information 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 Methanocaldococcus jannaschii JAL-1 ?
-
-
additional information 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 Mycobacterium tuberculosis H37Rv ?
-
-
additional information 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 Mycobacterium tuberculosis ATCC 25618 ?
-
-
additional information 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 Methanocaldococcus jannaschii JCM 10045 ?
-
-
phosphoenolpyruvate + GTP
-
 Mycobacterium tuberculosis enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
 ?
phosphoenolpyruvate + GTP
-
 Methanocaldococcus jannaschii enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
 ?
phosphoenolpyruvate + GTP
-
 Methanocaldococcus jannaschii NBRC 100440 enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
 ?
phosphoenolpyruvate + GTP
-
 Methanocaldococcus jannaschii DSM 2661 enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
 ?
phosphoenolpyruvate + GTP
-
 Methanocaldococcus jannaschii ATCC 43067 enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
 ?
phosphoenolpyruvate + GTP
-
 Methanocaldococcus jannaschii JAL-1 enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
 ?
phosphoenolpyruvate + GTP
-
 Mycobacterium tuberculosis H37Rv enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
 ?
phosphoenolpyruvate + GTP
-
 Mycobacterium tuberculosis ATCC 25618 enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
 ?
phosphoenolpyruvate + GTP
-
 Methanocaldococcus jannaschii JCM 10045 enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate
-
 ?

Synonyms

Synonyms Comment Organism
cofC
-
 Methanocaldococcus jannaschii
fbiD
-
 Mycobacterium tuberculosis
fbiD
-
 Methanocaldococcus jannaschii
guanylyltransferase
-
 Methanocaldococcus jannaschii
guanylyltransferase
-
 Mycobacterium tuberculosis
Mj-CofC
-
 Methanocaldococcus jannaschii
MJ0887
-
 Methanocaldococcus jannaschii
More cf. 2.7.7.68 Methanocaldococcus jannaschii
Mtb-FbiD
-
 Mycobacterium tuberculosis
Rv2983
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
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 Methanocaldococcus jannaschii
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 Mycobacterium tuberculosis
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 Methanocaldococcus jannaschii
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 Mycobacterium tuberculosis
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 Mycobacterium tuberculosis
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 Mycobacterium tuberculosis
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 Methanocaldococcus jannaschii
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 Mycobacterium tuberculosis