To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https
PROSITE documentation PDOC00581

Riboflavin synthase alpha chain lumazine-binding repeat profile





Description

Riboflavin synthase (RS-α) catalyzes the biosynthesis of riboflavin (vitamin B2) by dismutation of 6,7-dimethyl-8-(1'-D-ribityl)lumazine (Lum) (EC 2.5.1.9). Riboflavin synthases of bacteria and fungi are structurally and evolutionary related to antenna proteins involved in bioluminescence of marine bacteria [1,2]. These proteins seem to have evolved from the duplication of a domain of about 100 residues, the lumazine-binding repeat.

The 3D structure of RS-α, which is an asymmetric homotrimer, shows that both domains form a 6-stranded antiparallel β-barrel (see <PDB:1PKV>) [3], while a C-terminal helix is involved in trimerization. The Lum-binding domain of RS-α forms two Greek-key folds with the topology BBHBBBHB, where most of the substrate binding sites are located in β-strands (B) 4 and 5 and in helix (H) 2 [3,4,5].

Some proteins known to contain a lumazine-binding repeat:

  • Riboflavin synthase α chain (EC 2.5.1.9) (gene ribC in Escherichia coli, ribB in Bacillus subtilis and Photobacterium leiognathi, RIB5 in yeast). This enzyme synthesizes riboflavin from two molecules of Lum, a pteridine-derivative.
  • Photobacterium phosphoreum lumazine protein (LumP) (gene luxL). LumP is a protein that modulates the color of the bioluminescence emission of bacterial luciferase. In the presence of LumP, light emission is shifted to higher energy values (shorter wavelength). LumP binds non-covalently to 6,7-dimethyl-8-(1'-D-ribityl)lumazine.
  • Vibrio fischeri yellow fluorescent protein (YFP) (gene luxY). Like LumP, YFP modulates light emission but towards a longer wavelength. YFP binds non-covalently to FMN.

The profile we developed covers the entire lumazine-binding repeat.

Last update:

December 2005 / Pattern removed, profile added and text revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

LUMAZINE_BIND, PS51177; Riboflavin synthase alpha chain lumazine-binding repeat profile  (MATRIX)


References

1AuthorsO'Kane D.J., Woodward B., Lee J., Prasher D.C.
TitleBorrowed proteins in bacterial bioluminescence.
SourceProc. Natl. Acad. Sci. U.S.A. 88:1100-1104(1991).
PubMed ID1996310

2AuthorsO'Kane D.J., Prasher D.C.
TitleEvolutionary origins of bacterial bioluminescence.
SourceMol. Microbiol. 6:443-449(1992).
PubMed ID1560772

3AuthorsMeining W., Eberhardt S., Bacher A., Ladenstein R.
TitleThe structure of the N-terminal domain of riboflavin synthase in complex with riboflavin at 2.6A resolution.
SourceJ. Mol. Biol. 331:1053-1063(2003).
PubMed ID12927541

4AuthorsTruffault V., Coles M., Diercks T., Abelmann K., Eberhardt S., Luttgen H., Bacher A., Kessler H.
TitleThe solution structure of the N-terminal domain of riboflavin synthase.
SourceJ. Mol. Biol. 309:949-960(2001).
PubMed ID11399071
DOI10.1006/jmbi.2001.4683

5AuthorsGerhardt S., Schott A.K., Kairies N., Cushman M., Illarionov B., Eisenreich W., Bacher A., Huber R., Steinbacher S., Fischer M.
TitleStudies on the reaction mechanism of riboflavin synthase: X-ray crystal structure of a complex with 6-carboxyethyl-7-oxo-8-ribityllumazine.
SourceStructure 10:1371-1381(2002).
PubMed ID12377123



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)