Information on EC 1.14.13.240 - 2-polyprenylphenol 6-hydroxylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.240
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RECOMMENDED NAME
GeneOntology No.
2-polyprenylphenol 6-hydroxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-(all-trans-polyprenyl)phenol + NADPH + H+ + O2 = 3-(all-trans-polyprenyl)benzene-1,2-diol + NADP+ + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ubiquinol-10 biosynthesis (prokaryotic)
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ubiquinol-7 biosynthesis (prokaryotic)
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ubiquinol-8 biosynthesis (prokaryotic)
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ubiquinol-9 biosynthesis (prokaryotic)
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Ubiquinone and other terpenoid-quinone biosynthesis
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
2-(all-trans-polyprenyl)phenol,NADPH:oxygen oxidoreductase (6-hydroxylating)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-(all-trans-polyprenyl)phenol + NADPH + H+ + O2
3-(all-trans-polyprenyl)benzene-1,2-diol + NADP+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G301A/N303A
mutation of residues form the bottom of the isoalloxazine binding pocket, strongly impairs UbiI activity