BRENDA - Enzyme Database
show all sequences of 1.14.13.240

ubiI, a new gene in Escherichia coli coenzyme Q biosynthesis, is involved in aerobic C5-hydroxylation

Hajj Chehade, M.; Loiseau, L.; Lombard, M.; Pecqueur, L.; Ismail, A.; Smadja, M.; Golinelli-Pimpaneau, B.; Mellot-Draznieks, C.; Hamelin, O.; Aussel, L.; Kieffer-Jaquinod, S.; Labessan, N.; Barras, F.; Fontecave, M.; Pierrel, F.; J. Biol. Chem. 288, 20085-20092 (2013)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
-
Escherichia coli
Crystallization (Commentary)
Crystallization (Commentary)
Organism
crystal structure of a truncated form of UbiI. Residues of the flavin binding pocket of UbiI are important for activity
Escherichia coli
Engineering
Protein Variants
Commentary
Organism
G301A/N303A
mutation of residues form the bottom of the isoalloxazine binding pocket, strongly impairs UbiI activity
Escherichia coli
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
P25535
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
2-(all-trans-polyprenyl)phenol + NADPH + H+ + O2
-
745289
Escherichia coli
3-(all-trans-polyprenyl)benzene-1,2-diol + NADP+ + H2O
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
2-octaprenylphenol hydroxylase
-
Escherichia coli
ubiI
-
Escherichia coli
visC
-
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
-
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
-
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystal structure of a truncated form of UbiI. Residues of the flavin binding pocket of UbiI are important for activity
Escherichia coli
Engineering (protein specific)
Protein Variants
Commentary
Organism
G301A/N303A
mutation of residues form the bottom of the isoalloxazine binding pocket, strongly impairs UbiI activity
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
2-(all-trans-polyprenyl)phenol + NADPH + H+ + O2
-
745289
Escherichia coli
3-(all-trans-polyprenyl)benzene-1,2-diol + NADP+ + H2O
-
-
-
?
General Information
General Information
Commentary
Organism
physiological function
a strain deficient in ubiI has a low level of coenzyme Q and accumulates 3-octaprenyl-4-hydroxyphenol. UbiI is only implicated in aerobic Q biosynthesis. C5-hydroxylation reaction is totally abolished in a strain lacking both UbiF and UbiI. UbiI partially complements the C5-hydroxylation defect of Saccharomyces cerevisiae cells lacking COQ6
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
physiological function
a strain deficient in ubiI has a low level of coenzyme Q and accumulates 3-octaprenyl-4-hydroxyphenol. UbiI is only implicated in aerobic Q biosynthesis. C5-hydroxylation reaction is totally abolished in a strain lacking both UbiF and UbiI. UbiI partially complements the C5-hydroxylation defect of Saccharomyces cerevisiae cells lacking COQ6
Escherichia coli
Other publictions for EC 1.14.13.240
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
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)
745829
Pelosi
Evolution of ubiquinone biosy ...
Neisseria meningitidis, Neisseria meningitidis ATCC 13091
mSystems
30
e00091
2016
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745289
Hajj Chehade
ubiI, a new gene in Escherich ...
Escherichia coli
J. Biol. Chem.
288
20085-20092
2013
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