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Gene Review

ubiA  -  p-hydroxybenzoate octaprenyltransferase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK4032, JW4000, cyr
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Disease relevance of ubiA


High impact information on ubiA

  • We now report that E. coli mutants defective in the hemA gene or in the ubiA-menA genes markedly accumulate the reduced form of DsbA during growth under the conditions of protoheme deprivation as well as ubiquinone/menaquinone deprivation [4].
  • The sdgG suppressor is likely a mutation in one of three genes: ubiC, ubiA or yjbI [5].
  • However, this strain had normal levels of 4-hydroxybenzoate octaprenyltransferase, the enzyme catalyzing the analogous prenylation reaction in ubiquinone biosynthesis, providing additional evidence that the two octaprenyltransferases are quite distinct [6].
  • Neither IS16 nor the ubiA mutant strain could produce alkaline phosphatase (in contrast to their parent strains) after 2 h of induction, thus showing Dsb- phenotypes [3].
  • Mutant complementation by plasmids showed that ubiA is located between malM and plsB [1].

Chemical compound and disease context of ubiA


Biological context of ubiA


Anatomical context of ubiA


Associations of ubiA with chemical compounds


Analytical, diagnostic and therapeutic context of ubiA


  1. The 92-min region of the Escherichia coli chromosome: location and cloning of the ubiA and alr genes. Lilley, P.E., Stamford, N.P., Vasudevan, S.G., Dixon, N.E. Gene (1993) [Pubmed]
  2. Mutations in aarE, the ubiA homolog of Providencia stuartii, result in high-level aminoglycoside resistance and reduced expression of the chromosomal aminoglycoside 2'-N-acetyltransferase. Paradise, M.R., Cook, G., Poole, R.K., Rather, P.N. Antimicrob. Agents Chemother. (1998) [Pubmed]
  3. Low ubiquinone content in Escherichia coli causes thiol hypersensitivity. Zeng, H., Snavely, I., Zamorano, P., Javor, G.T. J. Bacteriol. (1998) [Pubmed]
  4. Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells. Kobayashi, T., Kishigami, S., Sone, M., Inokuchi, H., Mogi, T., Ito, K. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  5. Isolation and characterization of suppressors of two Escherichia coli dnaG mutations, dnaG2903 and parB. Britton, R.A., Lupski, J.R. Genetics (1997) [Pubmed]
  6. Biosynthesis of bacterial menaquinones: the membrane-associated 1,4-dihydroxy-2-naphthoate octaprenyltransferase of Escherichia coli. Shineberg, B., Young, I.G. Biochemistry (1976) [Pubmed]
  7. Role of quinones in electron transport to oxygen and nitrate in Escherichia coli. Studies with a ubiA- menA- double quinone mutant. Wallace, B.J., Young, I.G. Biochim. Biophys. Acta (1977) [Pubmed]
  8. Active expression of the ubiA gene from E. coli in tobacco: influence of plant ER-specific signal peptides on the expression of a membrane-bound prenyltransferase in plant cells. Boehm, R., Sommer, S., Severin, K., Li, S.M., Heide, L. Transgenic Res. (2000) [Pubmed]
  9. Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase. Nichols, B.P., Green, J.M. J. Bacteriol. (1992) [Pubmed]
  10. Ubiquinone biosynthesis. Cloning of the genes coding for chorismate pyruvate-lyase and 4-hydroxybenzoate octaprenyl transferase from Escherichia coli. Siebert, M., Bechthold, A., Melzer, M., May, U., Berger, U., Schröder, G., Schröder, J., Severin, K., Heide, L. FEBS Lett. (1992) [Pubmed]
  11. Genetic engineering on shikonin biosynthesis: expression of the bacterial ubiA gene in Lithospermum erythrorhizon. Boehm, R., Sommer, S., Li, S.M., Heide, L. Plant Cell Physiol. (2000) [Pubmed]
  12. Modeling the E. coli 4-hydroxybenzoic acid oligoprenyltransferase ( ubiA transferase) and characterization of potential active sites. Bräuer, L., Brandt, W., Wessjohann, L.A. Journal of molecular modeling (Online) (2004) [Pubmed]
  13. Evidence that Escherichia coli ubiA product is a functional homolog of yeast COQ2, and the regulation of ubiA gene expression. Suzuki, K., Ueda, M., Yuasa, M., Nakagawa, T., Kawamukai, M., Matsuda, H. Biosci. Biotechnol. Biochem. (1994) [Pubmed]
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