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Literature summary for 1.14.13.240 extracted from

  • 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 (2016), mSystems, 30, e00091 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.13.240

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis E0N696
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Neisseria meningitidis ATCC 13091 E0N696
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-(all-trans-polyprenyl)phenol + NADPH + H+ + O2
-
 Neisseria meningitidis 3-(all-trans-polyprenyl)benzene-1,2-diol + NADP+ + H2O
-
 ?
2-(all-trans-polyprenyl)phenol + NADPH + H+ + O2
-
 Neisseria meningitidis ATCC 13091 3-(all-trans-polyprenyl)benzene-1,2-diol + NADP+ + H2O
-
 ?

Synonyms

Synonyms Comment Organism
HMPREF0602_0026
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 Neisseria meningitidis
ubiM
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 Neisseria meningitidis

General Information

General Information Comment Organism
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 Neisseria meningitidis