Difference between revisions of "RibC"

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|style="background:#ABCDEF;" align="center"|'''Function''' || FAD biosynthesis  
 
|style="background:#ABCDEF;" align="center"|'''Function''' || FAD biosynthesis  
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/riboflavin.html Riboflavin and FAD synthesis]'''
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 35 kDa, 8.3   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 35 kDa, 8.3   

Revision as of 09:46, 16 February 2010

  • Description: riboflavin kinase / FAD synthase

Gene name ribC
Synonyms
Essential no
Product riboflavin kinase / FAD synthase
Function FAD biosynthesis
Metabolic function and regulation of this protein in SubtiPathways:
Riboflavin and FAD synthesis
MW, pI 35 kDa, 8.3
Gene length, protein length 948 bp, 316 aa
Immediate neighbours truB, rpsO
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RibC context.gif
This image was kindly provided by SubtiList



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:
  • Interactions:
  • Localization:

Database entries

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

Additional information

Expression and regulation

  • Operon:
  • 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

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)