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Gene Review

birA  -  bifunctional biotin-[acetylCoA...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3965, JW3941, bioR, dhbB
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Disease relevance of birA


High impact information on birA


Biological context of birA


Associations of birA with chemical compounds

  • For the several birA mutants examined, there appeared to be no direct correlation between effects on minimum biotin requirement and alterations in repressibility, suggesting a possible dual function for the gene [11].
  • The birA protein has been purified to homogeneity in a three-step process involving chromatography on phosphocellulose and hydroxyapatite columns [7].
  • BCCP becomes an active substrate for carboxylation and carboxyl transfer, after biotinylation of its canonical lysine residue by biotin protein ligase (BPL) [12].


  1. Isolation of a cDNA encoding human holocarboxylase synthetase by functional complementation of a biotin auxotroph of Escherichia coli. León-Del-Rio, A., Leclerc, D., Akerman, B., Wakamatsu, N., Gravel, R.A. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  2. Cloning and characterization of the Bacillus subtilis birA gene encoding a repressor of the biotin operon. Bower, S., Perkins, J., Yocum, R.R., Serror, P., Sorokin, A., Rahaim, P., Howitt, C.L., Prasad, N., Ehrlich, S.D., Pero, J. J. Bacteriol. (1995) [Pubmed]
  3. Stabilization of the biotinoyl domain of Escherichia coli acetyl-CoA carboxylase by interactions between the attached biotin and the protruding "thumb" structure. Solbiati, J., Chapman-Smith, A., Cronan, J.E. J. Biol. Chem. (2002) [Pubmed]
  4. Mutational analysis of protein substrate presentation in the post-translational attachment of biotin to biotin domains. Polyak, S.W., Chapman-Smith, A., Mulhern, T.D., Cronan, J.E., Wallace, J.C. J. Biol. Chem. (2001) [Pubmed]
  5. Molecular recognition in a post-translational modification of exceptional specificity. Mutants of the biotinylated domain of acetyl-CoA carboxylase defective in recognition by biotin protein ligase. Chapman-Smith, A., Morris, T.W., Wallace, J.C., Cronan, J.E. J. Biol. Chem. (1999) [Pubmed]
  6. Crystallization of the bifunctional biotin operon repressor. Brennan, R.G., Vasu, S., Matthews, B.W., Otsuka, A.J. J. Biol. Chem. (1989) [Pubmed]
  7. Overproduction and rapid purification of the biotin operon repressor from Escherichia coli. Buoncristiani, M.R., Otsuka, A.J. J. Biol. Chem. (1988) [Pubmed]
  8. DNA-binding and enzymatic domains of the bifunctional biotin operon repressor (BirA) of Escherichia coli. Buoncristiani, M.R., Howard, P.K., Otsuka, A.J. Gene (1986) [Pubmed]
  9. Evaluation of two novel tag-based labelling technologies for site-specific modification of proteins. Tirat, A., Freuler, F., Stettler, T., Mayr, L.M., Leder, L. Int. J. Biol. Macromol. (2006) [Pubmed]
  10. Structure of a putative lipoate protein ligase from Thermoplasma acidophilum and the mechanism of target selection for post-translational modification. McManus, E., Luisi, B.F., Perham, R.N. J. Mol. Biol. (2006) [Pubmed]
  11. Use of bio-lac fusion strains to study regulation of biotin biosynthesis in Escherichia coli. Barker, D.F., Campbell, A.M. J. Bacteriol. (1980) [Pubmed]
  12. A unique biotin carboxyl carrier protein in archaeon Sulfolobus tokodaii. Li, Y.Q., Sueda, S., Kondo, H., Kawarabayasi, Y. FEBS Lett. (2006) [Pubmed]
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