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Literature summary for 1.14.13.240 extracted from

  • 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 (2013), J. Biol. Chem., 288, 20085-20092 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of a truncated form of UbiI. Residues of the flavin binding pocket of UbiI are important for activity Escherichia coli

Protein Variants

Protein Variants Comment Organism
G301A/N303A mutation of residues form the bottom of the isoalloxazine binding pocket, strongly impairs UbiI activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P25535
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-(all-trans-polyprenyl)phenol + NADPH + H+ + O2
-
 Escherichia coli 3-(all-trans-polyprenyl)benzene-1,2-diol + NADP+ + H2O
-
 ?

Synonyms

Synonyms Comment Organism
2-octaprenylphenol hydroxylase
-
 Escherichia coli
ubiI
-
 Escherichia coli
visC
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Escherichia coli

General Information

General Information Comment 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