RibH

• Description: riboflavin synthase (beta subunit)
  
  

Gene name	ribH
Synonyms
Essential	no
Product	riboflavin synthase (beta subunit)
Function	riboflavin biosynthesis
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 This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU23250

Database entries

• 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:

• Cofactor(s):

• Effectors of protein activity:

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

• Localization:

Database entries

• 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: ypuE-ribD-ribE-ribA-ribH-ribT 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

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)