RibC

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  • Description: riboflavin kinase / FAD synthase

Gene name ribC
Synonyms
Essential yes PubMed
Product riboflavin kinase / FAD synthase
Function FAD biosynthesis
Gene expression levels in SubtiExpress: ribC
Metabolic function and regulation of this protein in SubtiPathways:
Riboflavin / FAD
MW, pI 35 kDa, 8.3
Gene length, protein length 948 bp, 316 aa
Immediate neighbours truB, rpsO
Sequences Protein DNA DNA_with_flanks
Genetic context
RibC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RibC expression.png















Categories containing this gene/protein

biosynthesis of cofactors, essential genes

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU16670

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + riboflavin = ADP + FMN (according to Swiss-Prot)
  • Protein family: ribF family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1S4M (from Thermotoga maritima, 33% identity, 54% similarity) PubMed
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Kosei Tanaka, Christopher S Henry, Jenifer F Zinner, Edmond Jolivet, Matthew P Cohoon, Fangfang Xia, Vladimir Bidnenko, S Dusko Ehrlich, Rick L Stevens, Philippe Noirot
Building the repertoire of dispensable chromosome regions in Bacillus subtilis entails major refinement of cognate large-scale metabolic model.
Nucleic Acids Res: 2013, 41(1);687-99
[PubMed:23109554] [WorldCat.org] [DOI] (I p)

Weiru Wang, Rosalind Kim, Hisao Yokota, Sung-Hou Kim
Crystal structure of flavin binding to FAD synthetase of Thermotoga maritima.
Proteins: 2005, 58(1);246-8
[PubMed:15468322] [WorldCat.org] [DOI] (I p)