4.1.1.98: 4-hydroxy-3-polyprenylbenzoate decarboxylase

This is an abbreviated version!
For detailed information about 4-hydroxy-3-polyprenylbenzoate decarboxylase, go to the full flat file.

Reaction

Synonyms

3-octaprenyl-4-hydroxybenzoate carboxy-lyase, 3-octaprenyl-4-hydroxybenzoate decarboxylase, 4-hydroxy-3-solanesylbenzoate decarboxylase, CpsUbiX, flavin mononucleotide-dependent aromatic acid decarboxylase, FMN-dependent aromatic acid decarboxylase, PA0254, PAD1, slr1099, ubiD, ubiX, yigC

ECTree

     4 Lyases

         4.1 Carbon-carbon lyases

             4.1.1 Carboxy-lyases

                4.1.1.98 4-hydroxy-3-polyprenylbenzoate decarboxylase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
7	Activating Compound
6209	AA Sequence
7	Cloned(Commentary)
6	Cofactor
6	Crystallization (Commentary)
6	General Information
2	Inhibitors
2	Localization
3	Metals/Ions
8	Molecular Weight [Da]
3	Natural Substrates/ Products (Substrates)
15	Organism
9	Pathway
12	PDB ID
1	pH Optimum
2	pI Value
3	Protein Variants
5	Purification (Commentary)
1	Reaction
11	Reference
14	Substrates and Products (Substrate)
5	Subunits
28	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]

Crystallization

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Crystallization on EC 4.1.1.98 - 4-hydroxy-3-polyprenylbenzoate decarboxylase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide Go to Crystallization (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

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

Colwellia psychrerythraea

Q489U8

746643

sitting drop vapor diffusion method, using 0.1 M trisodium citrate pH 5.4, 0.5 M ammonium sulfate, 1.2 M lithium sulfate

Colwellia psychrerythraea

Q489U8

728916

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)

Colwellia psychrerythraea

Q489U8

749310

hanging drop vapor diffusion method, using 15% (w/v) PEG 4000, 0.2 M LiSO4, and 0.1 M Hepes buffer (pH 7.0)

Escherichia coli

P69772

730891

structures of holoUbiD reveal a relatively open active site potentially occluded from solvent through domain motion

Escherichia coli

P0AAB4

748226

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

Pseudomonas aeruginosa

-

730732