Difference between revisions of "RibH"

From SubtiWiki
Jump to: navigation, search
m (Reverted edits by 134.76.70.252 (talk) to last revision by Jstuelk)
Line 103: Line 103:
 
* '''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]] {{PubMed|8159171}}
+
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ribH_2427892_2428356_-1 ribH] {{PubMed|22383849}}
 +
 
 +
* '''Sigma factor:''' [[SigA]] {{PubMed|8159171}}
  
 
* '''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 09:19, 16 April 2012

  • Description: riboflavin synthase (beta subunit)

Gene name ribH
Synonyms
Essential no
Product riboflavin synthase (beta subunit)
Function riboflavin biosynthesis
Interactions involving this protein in SubtInteract: RibH
Metabolic function and regulation of this protein in SubtiPathways:
Riboflavin / FAD
MW, pI 16 kDa, 5.196
Gene length, protein length 462 bp, 154 aa
Immediate neighbours ribT, ribA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RibH 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: BSU23250

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine (according to Swiss-Prot)
  • Protein family: DMRL synthase 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

  • 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)

K Ritsert, R Huber, D Turk, R Ladenstein, K Schmidt-Bäse, A Bacher
Studies on the lumazine synthase/riboflavin synthase complex of Bacillus subtilis: crystal structure analysis of reconstituted, icosahedral beta-subunit capsids with bound substrate analogue inhibitor at 2.4 A resolution.
J Mol Biol: 1995, 253(1);151-67
[PubMed:7473709] [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)

H C Ludwig, F Lottspeich, A Henschen, R Ladenstein, A Bacher
Heavy riboflavin synthase of Bacillus subtilis. Primary structure of the beta subunit.
J Biol Chem: 1987, 262(3);1016-21
[PubMed:3100522] [WorldCat.org] (P p)