Difference between revisions of "RibA"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
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=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The protein=
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''  
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* '''[[Domains]]:'''  
  
 
* '''Modification:'''
 
* '''Modification:'''
  
* '''Cofactor(s):'''
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* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ribAB_2428389_2429585_-1 ribA] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ribAB_2428389_2429585_-1 ribA] {{PubMed|22383849}}
  
* '''Sigma factor:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/8159171 PubMed]
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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]
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=References=
 
=References=
  
<pubmed> 19583770 12456892,15808508,, 8159171, 7934829, 7934830 16115872 23270261 </pubmed>
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<pubmed> 19583770 12456892,15808508,, 8159171, 7934829, 7934830 16115872 23270261 24442413 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 09:57, 21 January 2014

  • Description: GTP cyclohydrolase II/ 3,4-dihydroxy-2-butanone 4-phosphate synthase

Gene name ribA
Synonyms
Essential no
Product GTP cyclohydrolase II/ 3,4-dihydroxy-2-butanone 4-phosphate synthase
Function riboflavin biosynthesis
Gene expression levels in SubtiExpress: ribA
Metabolic function and regulation of this protein in SubtiPathways:
ribA
MW, pI 43 kDa, 5.582
Gene length, protein length 1194 bp, 398 aa
Immediate neighbours ribH, ribE
Sequences Protein DNA DNA_with_flanks
Genetic context
RibA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RibA expression.png















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: BSU23260

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure: 2BZ0 (from E. coli, 54% identity, 69% similarity to the C-terminal domain) PubMed
  • 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

Markus Birkenmeier, Susanne Neumann, Thorsten Röder
Kinetic modeling of riboflavin biosynthesis in Bacillus subtilis under production conditions.
Biotechnol Lett: 2014, 36(5);919-28
[PubMed:24442413] [WorldCat.org] [DOI] (I p)

S A Skliarova, R A Kreneva, D A Perumov, A S Mironov
[The characterization of internal promoters in the Bacillus subtilis riboflavin biosynthesis operon].
Genetika: 2012, 48(10);1133-41
[PubMed:23270261] [WorldCat.org] (P p)

Martin Lehmann, Simone Degen, Hans-Peter Hohmann, Markus Wyss, Adelbert Bacher, Nicholas Schramek
Biosynthesis of riboflavin. Screening for an improved GTP cyclohydrolase II mutant.
FEBS J: 2009, 276(15);4119-29
[PubMed:19583770] [WorldCat.org] [DOI] (I p)

Jingshan Ren, Masayo Kotaka, Michael Lockyer, Heather K Lamb, Alastair R Hawkins, David K Stammers
GTP cyclohydrolase II structure and mechanism.
J Biol Chem: 2005, 280(44);36912-9
[PubMed:16115872] [WorldCat.org] [DOI] (P p)

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)

A Sorokin, E Zumstein, V Azevedo, S D Ehrlich, P Serror
The organization of the Bacillus subtilis 168 chromosome region between the spoVA and serA genetic loci, based on sequence data.
Mol Microbiol: 1993, 10(2);385-95
[PubMed:7934829] [WorldCat.org] [DOI] (P p)