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Gene Review

ribC  -  riboflavin synthase, alpha subunit

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK1658, JW1654, ribE
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Disease relevance of ribC

  • The ribC gene was hyperexpressed in recombinant E. coli strains to a level of about 30% of cellular protein [1].
  • Molecular analysis of riboflavin synthesis genes in Bartonella henselae and use of the ribC gene for differentiation of Bartonella species by PCR [2].
  • The ribC gene is adjacent to a cluster of four genes with similarity to the genes cbiMNQO of Salmonella typhimurium, which form part of the cob operon (this operon contains most of the genes involved in the biosynthesis of vitamin B12) [3].
  • DNA sequence analysis of this fragment revealed several ORFs, one of which encodes a polypeptide of 230 amino acids with up to 45% sequence identity with FAD synthetases from a number of micro-organisms, such as Corynebacterium ammoniagenes, E. coli and Pseudomonas fluorescens, and also to the ribC gene product of B. subtilis [4].
  • By expression of P. phosphoreum ribE in E. coli using the bacteriophage T7 promoter-RNA polymerase system, ribE was shown to code for riboflavin synthetase, which catalyzes the conversion of lumazine to riboflavin [5].

High impact information on ribC

  • The ribH gene specifying the lumazine synthase subunit can be expressed in high yield [6].
  • The amino acid sequence predicted by the ribC gene of M. thermoautotrophicum shows no similarity whatsoever to the sequences of riboflavin synthases of eubacteria and yeast [3].
  • The 3' end of the ribC gene is directly adjacent to the cfa gene, which codes for cyclopropane-fatty-acid synthase [1].

Associations of ribC with chemical compounds

  • Increased thermal stability of RibE on expression with RibH indicated that ribH coded for lumazine synthetase [5].

Analytical, diagnostic and therapeutic context of ribC

  • PCR amplification with primers derived from the ribC locus of B. henselae was used to isolate the corresponding DNA regions in B. bacilliformis, B. clarridgeiae, and B. quintana [2].
  • Sequence analysis of the ribC gene region in strains of B. henselae, which were previously shown to be genetically different, revealed that the ribC gene is highly conserved at the species level [2].


  1. Cloning, sequencing, mapping and hyperexpression of the ribC gene coding for riboflavin synthase of Escherichia coli. Eberhardt, S., Richter, G., Gimbel, W., Werner, T., Bacher, A. Eur. J. Biochem. (1996) [Pubmed]
  2. Molecular analysis of riboflavin synthesis genes in Bartonella henselae and use of the ribC gene for differentiation of Bartonella species by PCR. Bereswill, S., Hinkelmann, S., Kist, M., Sander, A. J. Clin. Microbiol. (1999) [Pubmed]
  3. Biosynthesis of riboflavin: an unusual riboflavin synthase of Methanobacterium thermoautotrophicum. Eberhardt, S., Korn, S., Lottspeich, F., Bacher, A. J. Bacteriol. (1997) [Pubmed]
  4. The ribR gene encodes a monofunctional riboflavin kinase which is involved in regulation of the Bacillus subtilis riboflavin operon. Solovieva, I.M., Kreneva, R.A., Leak, D.J., Perumov, D.A. Microbiology (Reading, Engl.) (1999) [Pubmed]
  5. Riboflavin synthesis genes are linked with the lux operon of Photobacterium phosphoreum. Lee, C.Y., O'Kane, D.J., Meighen, E.A. J. Bacteriol. (1994) [Pubmed]
  6. Enzyme catalysis via control of activation entropy: site-directed mutagenesis of 6,7-dimethyl-8-ribityllumazine synthase. Fischer, M., Haase, I., Kis, K., Meining, W., Ladenstein, R., Cushman, M., Schramek, N., Huber, R., Bacher, A. J. Mol. Biol. (2003) [Pubmed]
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