BRENDA - Enzyme Database
show all sequences of 1.3.8.17

Elongation of the poly-gamma-glutamate tail of F420 requires both domains of the F420 gamma-glutamyl ligase (FbiB) of Mycobacterium tuberculosis

Bashiri, G.; Rehan, A.; Sreebhavan, S.; Baker, H.; Baker, E.; Squire, C.; J. Biol. Chem. 291, 6882-6894 (2016) View publication on PubMedView publication on EuropePMC

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
-
Mycobacterium tuberculosis
Crystallization (Commentary)
Crystallization (Commentary)
Organism
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
Organism
Organism
UniProt
Commentary
Textmining
Mycobacterium tuberculosis
P9WP79
cf. EC 6.3.2.31, EC 6.3.2.34
-
Mycobacterium tuberculosis H37Rv
P9WP79
cf. EC 6.3.2.31, EC 6.3.2.34
-
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Mycobacterium tuberculosis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
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
General Information
General Information
Commentary
Organism
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
General Information (protein specific)
General Information
Commentary
Organism
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
Other publictions for EC 1.3.8.17
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Protein Variants
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
Synonyms
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)
760400
Braga
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Appl. Environ. Microbiol.
86
e00457
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-
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1
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-
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1
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1
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1
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1
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1
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1
1
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757742
Bashiri
A revised biosynthetic pathwa ...
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 700084
Nat. Commun.
10
1558
2019
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1
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3
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2
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2
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1
1
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760607
Ayikpoe
Spectroscopic and electrochem ...
Mycobacterium ulcerans, Mycobacterium ulcerans Agy99
Biochemistry
58
940-950
2019
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8
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4
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4
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2
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8
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4
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745359
Bashiri
Elongation of the poly-gamma- ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Biol. Chem.
291
6882-6894
2016
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1
1
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2
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1
1
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761374
Choi
Use of transposon Tn5367 muta ...
Mycobacterium tuberculosis variant bovis, Mycobacterium tuberculosis variant bovis ATCC BAA-935
J. Bacteriol.
183
7058-7066
2001
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2
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