Difference between revisions of "RibE"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ribA]]'', ''[[ribD]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ribA]]'', ''[[ribD]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU23270 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU23270 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU23270 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU23270 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU23270 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU23270 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:ribE_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:ribE_context.gif]]

Revision as of 10:37, 14 May 2013

  • Description: riboflavin synthase (alpha subunit)

Gene name ribE
Synonyms ribB
Essential no
Product riboflavin synthase (alpha subunit)
Function riboflavin biosynthesis
Gene expression levels in SubtiExpress: ribE
Interactions involving this protein in SubtInteract: RibE
Metabolic function and regulation of this protein in SubtiPathways:
Riboflavin / FAD
MW, pI 23 kDa, 5.845
Gene length, protein length 645 bp, 215 aa
Immediate neighbours ribA, ribD
Sequences Protein DNA DNA_with_flanks
Genetic context
RibE context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RibE 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: BSU23270

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:
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure: 1I8D (from E. coli, 36% identity, 59% similarity) PubMed, , 1RVV (the RibE)3-(RibH)60 lumazine synthase/riboflavin synthase complex) 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: GP203 (erm), available in the Stülke lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

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)

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)

D I Liao, Z Wawrzak, J C Calabrese, P V Viitanen, D B Jordan
Crystal structure of riboflavin synthase.
Structure: 2001, 9(5);399-408
[PubMed:11377200] [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)