PROSITE documentation PDOC00581Riboflavin synthase alpha chain lumazine-binding repeat profile
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.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | O'Kane D.J. Woodward B. Lee J. Prasher D.C. |
| Title | Borrowed proteins in bacterial bioluminescence. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 88:1100-1104(1991). | |
| PubMed ID | 1996310 |
| 2 | Authors | O'Kane D.J. Prasher D.C. |
| Title | Evolutionary origins of bacterial bioluminescence. | |
| Source | Mol. Microbiol. 6:443-449(1992). | |
| PubMed ID | 1560772 |
| 3 | Authors | Meining W. Eberhardt S. Bacher A. Ladenstein R. |
| Title | The structure of the N-terminal domain of riboflavin synthase in complex with riboflavin at 2.6A resolution. | |
| Source | J. Mol. Biol. 331:1053-1063(2003). | |
| PubMed ID | 12927541 |
| 4 | Authors | Truffault V. Coles M. Diercks T. Abelmann K. Eberhardt S. Luttgen H. Bacher A. Kessler H. |
| Title | The solution structure of the N-terminal domain of riboflavin synthase. | |
| Source | J. Mol. Biol. 309:949-960(2001). | |
| PubMed ID | 11399071 | |
| DOI | 10.1006/jmbi.2001.4683 |
| 5 | Authors | Gerhardt S. Schott A.K. Kairies N. Cushman M. Illarionov B. Eisenreich W. Bacher A. Huber R. Steinbacher S. Fischer M. |
| Title | Studies on the reaction mechanism of riboflavin synthase: X-ray crystal structure of a complex with 6-carboxyethyl-7-oxo-8-ribityllumazine. | |
| Source | Structure 10:1371-1381(2002). | |
| PubMed ID | 12377123 |
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