RibH

• Description: riboflavin synthase (beta subunit)
  
  

Gene name	ribH
Synonyms
Essential	no
Product	riboflavin synthase (beta subunit)
Function	riboflavin biosynthesis
Gene expression levels in SubtiExpress: ribH
Interactions involving this protein in SubtInteract: RibH
Metabolic function and regulation of this protein in SubtiPathways: ribH
MW, pI	16 kDa, 5.196
Gene length, protein length	462 bp, 154 aa
Immediate neighbours	ribT, ribA
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• BsubCyc: BSU23250

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • (RibE)3-(RibH)60, the lumazine synthase/riboflavin synthase complex PubMed

• Localization:

Database entries

• BsubCyc: BSU23250

• Structure: 1ZIS, 1RVV (the RibE)3-(RibH)60 lumazine synthase/riboflavin synthase complex) PubMed

• UniProt: P11998

• KEGG entry: [3]

• E.C. number: 2.5.1.9

Expression and regulation

• Operon: ribD-ribE-ribA-ribH-ribT PubMed

• Expression browser: ribH PubMed

• Sigma factor: SigA PubMed

• Regulation: expressed in the absence of FMN (FMN-box) PubMed

• 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:

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)

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)