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Literature summary extracted from

  • Bashiri, G.; Rehan, A.; Sreebhavan, S.; Baker, H.; Baker, E.; Squire, C.
    Elongation of the poly-gamma-glutamate tail of F420 requires both domains of the F420 gamma-glutamyl ligase (FbiB) of Mycobacterium tuberculosis (2016), J. Biol. Chem., 291, 6882-6894 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.8.17
-
 Mycobacterium tuberculosis
6.3.2.31
-
 Mycobacterium tuberculosis
6.3.2.31 expression in Escherichia coli and in Mycobacterium smegmatis Mycobacterium tuberculosis
6.3.2.34
-
 Mycobacterium tuberculosis
6.3.2.34 expression in Escherichia coli and in Mycobacterium smegmatis Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.8.17 structures of the C-terminal domain of FbiB in apo-, F420-0-, and FMN-bound states, displaying distinct sites for F420-0 and FMN ligands that partially overlap Mycobacterium tuberculosis
6.3.2.31 crystal structures of the C-terminal domain of FbiB in apo-, F420-0-, and FMN-bound states Mycobacterium tuberculosis
6.3.2.31 structures of the C-terminal domain of FbiB in apo-, F420-0-, and FMN-bound states, displaying distinct sites for F420-0 and FMN ligands that partially overlap Mycobacterium tuberculosis
6.3.2.34 crystal structures of the C-terminal domain of FbiB in apo-, F420-0-, and FMN-bound states Mycobacterium tuberculosis
6.3.2.34 structures of the C-terminal domain of FbiB in apo-, F420-0-, and FMN-bound states, displaying distinct sites for F420-0 and FMN ligands that partially overlap Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.2.31 Mn2+ highest activity in presence of both Na+ and Mn2+, assay in presence of 100mMNaCl, 5mMMnCl2 Mycobacterium tuberculosis
6.3.2.31 Na+ highest activity in presence of both Na+ and Mn2+, assay in presence of 100mMNaCl, 5mMMnCl2 Mycobacterium tuberculosis
6.3.2.34 Mn2+ highest activity in presence of both Na+ and Mn2+, assay in presence of 100 mM NaCl, 5 mM MnCl2 Mycobacterium tuberculosis
6.3.2.34 Na+ highest activity in presence of both Na+ and Mn2+, assay in presence of 100 mM NaCl, 5 mM MnCl2 Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
1.3.8.17 Mycobacterium tuberculosis P9WP79 cf. EC 6.3.2.31, EC 6.3.2.34
-
1.3.8.17 Mycobacterium tuberculosis H37Rv P9WP79 cf. EC 6.3.2.31, EC 6.3.2.34
-
6.3.2.31 Mycobacterium tuberculosis P9WP79
-
-
6.3.2.31 Mycobacterium tuberculosis P9WP79 cf. EC 1.3.8.17, EC 6.3.2.34
-
6.3.2.31 Mycobacterium tuberculosis ATCC 25618 P9WP79
-
-
6.3.2.31 Mycobacterium tuberculosis H37Rv P9WP79 cf. EC 1.3.8.17, EC 6.3.2.34
-
6.3.2.34 Mycobacterium tuberculosis P9WP79
-
-
6.3.2.34 Mycobacterium tuberculosis P9WP79 cf. EC 1.3.8.17, EC 6.3.2.31
-
6.3.2.34 Mycobacterium tuberculosis ATCC 25618 P9WP79
-
-
6.3.2.34 Mycobacterium tuberculosis H37Rv P9WP79 cf. EC 1.3.8.17, EC 6.3.2.31
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.31 GTP + coenzyme F420-0 + L-glutamate
-
 Mycobacterium tuberculosis GDP + phosphate + coenzyme F420-1
-
 ?
6.3.2.31 GTP + coenzyme F420-0 + L-glutamate
-
 Mycobacterium tuberculosis H37Rv GDP + phosphate + coenzyme F420-1
-
 ?
6.3.2.31 GTP + coenzyme F420-0 + L-glutamate
-
 Mycobacterium tuberculosis ATCC 25618 GDP + phosphate + coenzyme F420-1
-
 ?
6.3.2.31 additional information full-length FbiB adds multiple L-glutamate residues to F420-0 in vitro to produce F420-5, i.e. 5 L-glutamate residues in the poly-gamma-glutamate tail after 24 h, reactions of EC 6.3.2.31 and 6.3.2.34. Communication between the two domains of the protein is critical for full gamma-glutamyl ligase activity. No observed activity for dGTP, ATP, and dATP nucleotides Mycobacterium tuberculosis ?
-
 ?
6.3.2.31 additional information full-length FbiB adds multiple L-glutamate residues to F420-0 in vitro to produce F420-5, i.e. 5 L-glutamate residues in the poly-gamma-glutamate tail after 24 h, reactions of EC 6.3.2.31 and 6.3.2.34. Communication between the two domains of the protein is critical for full gamma-glutamyl ligase activity. No observed activity for dGTP, ATP, and dATP nucleotides Mycobacterium tuberculosis H37Rv ?
-
 ?
6.3.2.31 additional information full-length FbiB adds multiple L-glutamate residues to F420-0 in vitro to produce F420-5, i.e. 5 L-glutamate residues in the poly-gamma-glutamate tail after 24 h, reactions of EC 6.3.2.31 and 6.3.2.34. Communication between the two domains of the protein is critical for full gamma-glutamyl ligase activity. No observed activity for dGTP, ATP, and dATP nucleotides Mycobacterium tuberculosis ATCC 25618 ?
-
 ?
6.3.2.34 GTP + coenzyme F420-1 + L-glutamate
-
 Mycobacterium tuberculosis GDP + phosphate + coenzyme gamma-F420-2
-
 ?
6.3.2.34 GTP + coenzyme F420-1 + L-glutamate
-
 Mycobacterium tuberculosis H37Rv GDP + phosphate + coenzyme gamma-F420-2
-
 ?
6.3.2.34 GTP + coenzyme F420-1 + L-glutamate
-
 Mycobacterium tuberculosis ATCC 25618 GDP + phosphate + coenzyme gamma-F420-2
-
 ?
6.3.2.34 additional information full-length FbiB adds multiple L-glutamate residues to F420-0 in vitro to produce F420-5, i.e. 5 L-glutamate residues in the poly-gamma-glutamate tail after 24 h, reactions of EC 6.3.2.31 and 6.3.2.34. Communication between the two domains of the protein is critical for full gamma-glutamyl ligase activity. No observed activity for dGTP, ATP, and dATP nucleotides Mycobacterium tuberculosis ?
-
 ?
6.3.2.34 additional information full-length FbiB adds multiple L-glutamate residues to F420-0 in vitro to produce F420-5, i.e. 5 L-glutamate residues in the poly-gamma-glutamate tail after 24 h, reactions of EC 6.3.2.31 and 6.3.2.34. Communication between the two domains of the protein is critical for full gamma-glutamyl ligase activity. No observed activity for dGTP, ATP, and dATP nucleotides Mycobacterium tuberculosis H37Rv ?
-
 ?
6.3.2.34 additional information full-length FbiB adds multiple L-glutamate residues to F420-0 in vitro to produce F420-5, i.e. 5 L-glutamate residues in the poly-gamma-glutamate tail after 24 h, reactions of EC 6.3.2.31 and 6.3.2.34. Communication between the two domains of the protein is critical for full gamma-glutamyl ligase activity. No observed activity for dGTP, ATP, and dATP nucleotides Mycobacterium tuberculosis ATCC 25618 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.3.2.31 FbiB
-
 Mycobacterium tuberculosis
6.3.2.34 FbiB
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.2.31 37
-
 assay at Mycobacterium tuberculosis
6.3.2.34 37
-
 assay at Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.2.31 8.5
-
-
 Mycobacterium tuberculosis
6.3.2.34 8.5
-
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
1.3.8.17 physiological function FbiB produces cofactor F420 with predominantly 5-7 L-glutamate residues in the poly-gamma-glutamate tail, reactions of EC 6.3.2.31 and 6.3.2.34. The N-terminal domain of FbiB is homologous to CofE with an annotated gamma-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Communication between the two domains is critical for full gamma-glutamyl ligase activity Mycobacterium tuberculosis
6.3.2.31 physiological function FbiB produces cofactor F420 with predominantly 5-7 L-glutamate residues in the poly-gamma-glutamate tail, reactions of EC 6.3.2.31 and 6.3.2.34. The N-terminal domain of FbiB is homologous to CofE with an annotated gamma-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Communication between the two domains is critical for full gamma-glutamyl ligase activity Mycobacterium tuberculosis
6.3.2.34 physiological function FbiB produces cofactor F420 with predominantly 5-7 L-glutamate residues in the poly-gamma-glutamate tail, reactions of EC 6.3.2.31 and 6.3.2.34. The N-terminal domain of FbiB is homologous to CofE with an annotated gamma-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Communication between the two domains is critical for full gamma-glutamyl ligase activity Mycobacterium tuberculosis