Difference between revisions of "RibD"

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* '''Operon:'''  ''[[ypuE]]-[[ribD]]-[[ribE]]-[[ribA]]-[[ribH]]-[[ribT]]''  [http://www.ncbi.nlm.nih.gov/sites/entrez/8159171 PubMed]
 
* '''Operon:'''  ''[[ypuE]]-[[ribD]]-[[ribE]]-[[ribA]]-[[ribH]]-[[ribT]]''  [http://www.ncbi.nlm.nih.gov/sites/entrez/8159171 PubMed]
  
* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/8159171 PubMed]
+
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ribD_2430258_2431343_-1 ribD] {{PubMed|22383849}}
 +
 
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* '''Sigma factor:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/8159171 PubMed]
  
 
* '''Regulation:''' expressed in the absence of FMN ([[FMN-box]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/15808508 PubMed]
 
* '''Regulation:''' expressed in the absence of FMN ([[FMN-box]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/15808508 PubMed]

Revision as of 10:27, 16 April 2012

  • Description: 5-amino-6-(5-phosphoribosylamino)uracil reductase

Gene name ribD
Synonyms ribG
Essential no
Product 5-amino-6-(5-phosphoribosylamino)uracil reductase
Function riboflavin biosynthesis
Metabolic function and regulation of this protein in SubtiPathways:
Riboflavin / FAD
MW, pI 39 kDa, 6.079
Gene length, protein length 1083 bp, 361 aa
Immediate neighbours ribE, ypuE
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RibD context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

biosynthesis of cofactors

This gene is a member of the following regulons

FMN-box

The gene

Basic information

  • Locus tag: BSU23280

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + H2O = 5-amino-6-(5-phosphoribosylamino)uracil + NH3 (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulatory mechanism: FMN-box: riboswitch, mediates termination/ antitermination control of the operon, in the absence of FMN: antitermination, in the presence of FMN: termination PubMed
  • 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

J Kenneth Wickiser, Wade C Winkler, Ronald R Breaker, Donald M Crothers
The speed of RNA transcription and metabolite binding kinetics operate an FMN riboswitch.
Mol Cell: 2005, 18(1);49-60
[PubMed:15808508] [WorldCat.org] [DOI] (P p)

Wade C Winkler, Smadar Cohen-Chalamish, Ronald R Breaker
An mRNA structure that controls gene expression by binding FMN.
Proc Natl Acad Sci U S A: 2002, 99(25);15908-13
[PubMed:12456892] [WorldCat.org] [DOI] (P p)

V N Mironov, A S Kraev, M L Chikindas, B K Chernov, A I Stepanov, K G Skryabin
Functional organization of the riboflavin biosynthesis operon from Bacillus subtilis SHgw.
Mol Gen Genet: 1994, 242(2);201-8
[PubMed:8159171] [WorldCat.org] [DOI] (P p)

V Azevedo, A Sorokin, S D Ehrlich, P Serror
The transcriptional organization of the Bacillus subtilis 168 chromosome region between the spoVAF and serA genetic loci.
Mol Microbiol: 1993, 10(2);397-405
[PubMed:7934830] [WorldCat.org] [DOI] (P p)