Riboflavin synthase
Details
- Name
- Riboflavin synthase
- Synonyms
- 2.5.1.9
- ribE
- RS
- Gene Name
- ribC
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0012326|Riboflavin synthase MFTGIVQGTAKLVSIDEKPNFRTHVVELPDHMLDGLETGASVAHNGCCLTVTEINGNHVS FDLMKETLRITNLGDLKVGDWVNVERAAKFSDEIGGHLMSGHIMTTAEVAKILTSENNRQ IWFKVQDSQLMKYILYKGFIGIDGISLTVGEVTPTRFCVHLIPETLERTTLGKKKLGARV NIEIDPQTQAVVDTVERVLAARENAMNQPGTEA
- Number of residues
- 213
- Molecular Weight
- 23444.77
- Theoretical pI
- 5.88
- GO Classification
- Functionsoxidoreductase activity / riboflavin synthase activityProcessesriboflavin biosynthetic processComponentscytosol
- General Function
- Riboflavin synthase activity
- Specific Function
- Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil.
- Pfam Domain Function
- Lum_binding (PF00677)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0012327|Riboflavin synthase (ribC) ATGTTTACGGGGATTGTACAGGGCACCGCAAAACTGGTGTCGATTGACGAGAAACCAAAT TTTCGTACGCATGTGGTGGAGTTACCCGACCACATGCTGGACGGCCTGGAAACCGGTGCT TCCGTGGCGCATAACGGTTGCTGCCTGACCGTGACGGAAATTAACGGCAACCATGTCAGT TTTGACCTGATGAAAGAAACGTTACGCATTACCAATCTTGGCGATTTAAAAGTGGGGGAT TGGGTAAACGTTGAGCGTGCGGCGAAATTCAGTGATGAAATTGGCGGACACTTAATGTCA GGTCATATTATGACCACTGCTGAAGTGGCGAAAATATTAACCTCAGAAAATAATCGCCAG ATCTGGTTTAAAGTCCAGGATAGTCAGTTGATGAAATATATTCTGTACAAAGGATTTATT GGCATCGACGGTATTAGCCTGACCGTCGGCGAAGTCACGCCAACGCGTTTTTGCGTCCAT TTAATTCCGGAAACACTGGAACGCACGACTCTTGGGAAGAAAAAACTTGGCGCACGCGTC AACATTGAAATCGATCCACAAACTCAGGCAGTGGTAGATACGGTAGAACGTGTGCTGGCG GCACGAGAAAATGCCATGAATCAACCAGGCACAGAAGCCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0AFU8 UniProtKB Entry Name RISA_ECOLI GenBank Gene ID X69109 - General References
- Eberhardt S, Richter G, Gimbel W, Werner T, Bacher A: Cloning, sequencing, mapping and hyperexpression of the ribC gene coding for riboflavin synthase of Escherichia coli. Eur J Biochem. 1996 Dec 15;242(3):712-9. [Article]
- Hensel M, Shea JE, Baumler AJ, Gleeson C, Blattner F, Holden DW: Analysis of the boundaries of Salmonella pathogenicity island 2 and the corresponding chromosomal region of Escherichia coli K-12. J Bacteriol. 1997 Feb;179(4):1105-11. [Article]
- Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kasai H, Kashimoto K, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Horiuchi T, et al.: A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):363-77. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Truffault V, Coles M, Diercks T, Abelmann K, Eberhardt S, Luttgen H, Bacher A, Kessler H: The solution structure of the N-terminal domain of riboflavin synthase. J Mol Biol. 2001 Jun 15;309(4):949-60. [Article]
- Liao DI, Wawrzak Z, Calabrese JC, Viitanen PV, Jordan DB: Crystal structure of riboflavin synthase. Structure. 2001 May 9;9(5):399-408. [Article]
- Meining W, Eberhardt S, Bacher A, Ladenstein R: The structure of the N-terminal domain of riboflavin synthase in complex with riboflavin at 2.6A resolution. J Mol Biol. 2003 Aug 29;331(5):1053-63. [Article]