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3-octaprenyl-4-hydroxybenzoate
2-octaprenylphenol + CO2
4-hydroxy-3-farnesylbenzoate
? + CO2
-
highest activity with 4-hydroxy-3-farnesylbenzoate
-
-
?
4-hydroxy-3-geranylgeranylbenzoate
? + CO2
-
-
-
-
?
a 4-hydroxy-3-polyprenylbenzoate
a 2-polyprenylphenol + CO2
additional information
?
-
3-octaprenyl-4-hydroxybenzoate
2-octaprenylphenol + CO2
-
-
-
-
?
3-octaprenyl-4-hydroxybenzoate
2-octaprenylphenol + CO2
-
-
-
-
?
3-octaprenyl-4-hydroxybenzoate
2-octaprenylphenol + CO2
-
-
-
?
3-octaprenyl-4-hydroxybenzoate
2-octaprenylphenol + CO2
-
-
-
-
?
3-octaprenyl-4-hydroxybenzoate
2-octaprenylphenol + CO2
-
-
-
?
3-octaprenyl-4-hydroxybenzoate
2-octaprenylphenol + CO2
-
-
-
-
?
a 4-hydroxy-3-polyprenylbenzoate
a 2-polyprenylphenol + CO2
-
-
-
?
a 4-hydroxy-3-polyprenylbenzoate
a 2-polyprenylphenol + CO2
-
-
-
?
a 4-hydroxy-3-polyprenylbenzoate
a 2-polyprenylphenol + CO2
-
-
-
-
?
additional information
?
-
analysis of the conformational changes upon FMN binding and the enzymatic mechanism at the molecular level, overview
-
-
?
additional information
?
-
-
very low specific activity with 4-hydroxy-3-octaprenylbenzoate
-
-
?
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evolution
UbiX belongs to the FMN-dependent decarboxylase family
physiological function
-
the enzyme is required for production of coenzyme Q8 and growth on succinate media
malfunction
-
disruption of the slr1099 gene results in reduced growth rates and plastoquinone contents
malfunction
-
the Escherichia coli ubiX null mutant accumulates 4-hydroxy-3-octaprenylbenzoic acid, a coenzyme Q8 precursor, and shows decreased UbiG O-methyltransferase activity
metabolism
-
the enzyme is involved in the decarboxylation step in coenzyme Q biosynthesis
metabolism
a set of enzymes, UbiA, UbiB, UbiC, UbiD, UbiE, UbiF, UbiG, UbiH and UbiX, catalyze the synthesis of ubiquinone from the compound chorismate. Enzyme UbiX catalyzes and regulates ubiquinone biosynthesis
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purified recombinant His6-tagged wild-type (FMN-bound) and V47S mutant (FMN-free) enzymes, hanging drop vapour diffusion method, mixing of 800 nl of 21 mg/ml protein solution with 800 nl of reservoir solution containing 200 mM sodium chloride, 100 mM potassium phosphate monobasic/sodium phosphate dibasic, pH 5.8, and 11% w/v PEG 8000, for the wild-type enzyme and 0.1 M trisodium citrate, pH 5.4, 0.5 M ammonium sulfate, and 1.2 M lithium sulfate for the mutant enzyme, 20°C, 3 days, method optimization, X-ray diffraction structrue determination and analysis at 2.0 A and 1.76 A resolution, respectively
sitting drop vapor diffusion method, using 0.1 M trisodium citrate pH 5.4, 0.5 M ammonium sulfate, 1.2 M lithium sulfate
structures of an FMN-bound wild type form and an FMN-unbound V47S mutant form. UbiX is a dodecameric enzyme, and each monomer possesses a typical Rossmann-fold structure. The FMN-binding domain of UbiX is composed of three neighboring subunits. The highly conserved Gly15, Ser41, Val47, and Tyr171 residues play important roles in FMN binding. The FMN-bound wild type form and the FMN-free form show a significant conformational difference in the C-terminal loop region (comprising residues 170-176 and 195-206)
hanging drop vapor diffusion method, using 15% (w/v) PEG 4000, 0.2 M LiSO4, and 0.1 M Hepes buffer (pH 7.0)
structures of holoUbiD reveal a relatively open active site potentially occluded from solvent through domain motion
sitting drop vapor diffusion method, using 1 M (NH4)2SO4, 0.1 M Bis-Tris, pH 5.5, 1% (w/v) PEG 3350 or 0.1 M HEPES, pH 7.5, 0.2 M MgCl2, 10% (w/v) PEG 400
-
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Pfaff, C.; Glindemann, N.; Gruber, J.; Frentzen, M.; Sadre, R.
Chorismate pyruvate-lyase and 4-hydroxy-3-solanesylbenzoate decarboxylase are required for plastoquinone biosynthesis in the cyanobacterium Synechocystis sp. PCC6803
J. Biol. Chem.
289
2675-2686
2014
Synechocystis sp.
brenda
Liu, J.; Liu, J.H.
Ubiquinone (coenzyme Q) biosynthesis in Chlamydophila pneumoniae AR39: identification of the ubiD gene
Acta Biochim. Biophys. Sin. (Shanghai)
38
725-730
2006
Chlamydia pneumoniae, Chlamydia pneumoniae AR39
brenda
Do, H.; Lee, C.W.; Han, S.J.; Lee, S.G.; Kim, H.J.; Park, H.; Lee, J.H.
Purification, crystallization and preliminary X-ray crystallographic studies of FMN-bound and FMN-free forms of aromatic acid decarboxylase (CpsUbiX) from the psychrophilic bacterium Colwellia psychrerythraea 34H
Acta Crystallogr. Sect. F
70
215-220
2014
Colwellia psychrerythraea (Q489U8)
brenda
Gulmezian, M.; Hyman, K.R.; Marbois, B.N.; Clarke, C.F.; Javor, G.T.
The role of UbiX in Escherichia coli coenzyme Q biosynthesis
Arch. Biochem. Biophys.
467
144-153
2007
Escherichia coli
brenda
Leppik, R.; Young, I.; Gibson, F.
Membrane associated reactions in ubiquinone biosynthesis in Escherichia coli. 3-Octaprenyl-4-hydroxybenzoate carboxy lyase
Biochim. Biophys. Acta
436
800-810
1976
Escherichia coli
brenda
Jacewicz, A.; Izumi, A.; Brunner, K.; Schnell, R.; Schneider, G.
Structural insights into the UbiD protein family from the crystal structure of PA0254 from Pseudomonas aeruginosa
PLoS ONE
8
e63161
2013
Pseudomonas aeruginosa
brenda
Rangarajan, E.S.; Li, Y.; Iannuzzi, P.; Tocilj, A.; Hung, L.W.; Matte, A.; Cygler, M.
Crystal structure of a dodecameric FMN-dependent UbiX-like decarboxylase (Pad1) from Escherichia coli O157: H7
Protein Sci.
13
3006-3016
2004
Escherichia coli (P69772)
brenda
Do, H.; Lee, C.W.; Han, S.J.; Lee, S.G.; Kim, H.J.; Park, H.; Lee, J.H.
Purification, crystallization and preliminary X-ray crystallographic studies of FMN-bound and FMN-free forms of aromatic acid decarboxylase (CpsUbiX) from the psychrophilic bacterium Colwellia psychrerythraea 34H
Acta Crystallogr. Sect. F
70
215-220
2014
Colwellia psychrerythraea (Q489U8)
brenda
Marshall, S.; Fisher, K.; Cheallaigh, A.; White, M.; Payne, K.; Parker, D.; Rigby, S.; Leys, D.
Oxidative maturation and structural characterization of prenylated FMN binding by UbiD, a decarboxylase involved in bacterial ubiquinone biosynthesis
J. Biol. Chem.
292
4623-4637
2017
Escherichia coli (P0AAB4)
brenda
Do, H.; Kim, S.; Lee, C.; Kim, H.; Park, H.; Kim, H.; Park, H.; Park, H.; Lee, J.
Crystal structure of UbiX, an aromatic acid decarboxylase from the psychrophilic bacterium Colwellia psychrerythraea that undergoes FMN-induced conformational changes
Sci. Rep.
5
8196
2015
Colwellia psychrerythraea (Q489U8), Colwellia psychrerythraea
brenda