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Information on EC 1.14.13.240 - 2-polyprenylphenol 6-hydroxylase and Organism(s) Escherichia coli and UniProt Accession P25535

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IUBMB Comments
Contains FAD. The enzyme from the bacterium Escherichia coli (UbiI) catalyses the first hydroxylation during the aerobic biosynthesis of ubiquinone. The enzyme from the bacterium Neisseria meningitidis (UbiM) can also catalyse the two additional hydroxylations that occur in the pathway (cf. EC 1.14.99.60, 3-demethoxyubiquinol 3-hydroxylase).
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Escherichia coli
UNIPROT: P25535
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
2-octaprenylphenol hydroxylase, HMPREF0602_0026, ubiI, ubiM, visC, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-octaprenylphenol hydroxylase
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ubiI
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ubiM
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
2-(all-trans-polyprenyl)phenol,NADPH:oxygen oxidoreductase (6-hydroxylating)
Contains FAD. The enzyme from the bacterium Escherichia coli (UbiI) catalyses the first hydroxylation during the aerobic biosynthesis of ubiquinone. The enzyme from the bacterium Neisseria meningitidis (UbiM) can also catalyse the two additional hydroxylations that occur in the pathway (cf. EC 1.14.99.60, 3-demethoxyubiquinol 3-hydroxylase).
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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
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
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G301A/N303A
mutation of residues form the bottom of the isoalloxazine binding pocket, strongly impairs UbiI activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team