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Enzyme Nomenclature
Information on EC 1.14.13.240 - 2-polyprenylphenol 6-hydroxylase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.13.240
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RECOMMENDED NAME
GeneOntology No.
2-polyprenylphenol 6-hydroxylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-(all-trans-polyprenyl)phenol + NADPH + H+ + O2 = 3-(all-trans-polyprenyl)benzene-1,2-diol + NADP+ + H2O
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
2-(all-trans-polyprenyl)phenol,NADPH:oxygen oxidoreductase (6-hydroxylating)
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
physiological function
expression of UbiM complements C-1/C-5/C-6 hydroxylation defects in Escherichia coli. Neisseria meningitidis does not contain ubiH, ubiF, ubiI, ubiL, or coq7 genes but possesses instead a single ubiquinone hydroxylase-encoding gene, i.e. UbiM. UbiM may perform all three hydroxylation reactions of the ubiquinone biosynthetic pathway in Neisseria meningitidis
physiological function
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expression of UbiM complements C-1/C-5/C-6 hydroxylation defects in Escherichia coli. Neisseria meningitidis does not contain ubiH, ubiF, ubiI, ubiL, or coq7 genes but possesses instead a single ubiquinone hydroxylase-encoding gene, i.e. UbiM. UbiM may perform all three hydroxylation reactions of the ubiquinone biosynthetic pathway in Neisseria meningitidis
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-(all-trans-polyprenyl)phenol + NADPH + H+ + O2
3-(all-trans-polyprenyl)benzene-1,2-diol + NADP+ + H2O
2-(all-trans-polyprenyl)phenol + NADPH + H+ + O2
3-(all-trans-polyprenyl)benzene-1,2-diol + NADP+ + H2O
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-
-
?
2-(all-trans-polyprenyl)phenol + NADPH + H+ + O2
3-(all-trans-polyprenyl)benzene-1,2-diol + NADP+ + H2O
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-
-
?
2-(all-trans-polyprenyl)phenol + NADPH + H+ + O2
3-(all-trans-polyprenyl)benzene-1,2-diol + NADP+ + H2O
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-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of a truncated form of UbiI. Residues of the flavin binding pocket of UbiI are important for activity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G301A/N303A
mutation of residues form the bottom of the isoalloxazine binding pocket, strongly impairs UbiI activity
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.240)
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