RibC

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis of cofactors, essential genes

The gene

Basic information

• Locus tag: BSU16670

Phenotypes of a mutant

• essential PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions:

• Localization:

Database entries

• Structure: 1S4M (from Thermotoga maritima, 33% identity, 54% similarity) PubMed

• UniProt: P54575

• KEGG entry: [2]

• E.C. number: 2.7.1.26, 2.7.7.2

Expression and regulation

• Operon:

• Expression browser: ribC PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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)