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Information on EC 1.14.13.240 - 2-polyprenylphenol 6-hydroxylase for references in articles please use BRENDA:EC1.14.13.240Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The enzyme appears in viruses and cellular organisms
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2-polyprenylphenol 6-hydroxylase
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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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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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2-(all-trans-polyprenyl)phenol,NADPH:oxygen oxidoreductase (6-hydroxylating)
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2-octaprenylphenol hydroxylase
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HMPREF0602_0026
gene name
HMPREF0602_0026
gene name
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ubiI
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gene name
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ubiM
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gene name
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UniProt
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UniProt
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UniProt
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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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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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crystal structure of a truncated form of UbiI. Residues of the flavin binding pocket of UbiI are important for activity
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G301A/N303A
mutation of residues form the bottom of the isoalloxazine binding pocket, strongly impairs UbiI activity
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UBII_ECOLI
Escherichia coli (strain K12)
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44245
Swiss-Prot
E0N696_NEIME
430
47675
TrEMBL
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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.
ubiI, a new gene in Escherichia coli coenzyme Q biosynthesis, is involved in aerobic C5-hydroxylation
J. Biol. Chem.
288
20085-20092
2013
Escherichia coli (P25535)
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Pelosi, L.; Ducluzeau, A.L.; Loiseau, L.; Barras, F.; Schneider, D.; Junier, I.; Pierrel, F.
Evolution of ubiquinone biosynthesis multiple proteobacterial enzymes with various regioselectivities to catalyze three contiguous aromatic hydroxylation reactions
mSystems
30
e00091
2016
Neisseria meningitidis (E0N696), Neisseria meningitidis ATCC 13091 (E0N696)
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