Riboflavin synthase

NameRiboflavin synthase
Synonyms
  • 2.5.1.9
  • ribE
  • RS
Gene NameribC
OrganismEscherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0012326|Riboflavin synthase
MFTGIVQGTAKLVSIDEKPNFRTHVVELPDHMLDGLETGASVAHNGCCLTVTEINGNHVS
FDLMKETLRITNLGDLKVGDWVNVERAAKFSDEIGGHLMSGHIMTTAEVAKILTSENNRQ
IWFKVQDSQLMKYILYKGFIGIDGISLTVGEVTPTRFCVHLIPETLERTTLGKKKLGARV
NIEIDPQTQAVVDTVERVLAARENAMNQPGTEA
Number of residuesNone
Molecular Weight23444.77
Theoretical pI5.88
GO Classification
Functions
  • oxidoreductase activity
  • riboflavin synthase activity
Processes
  • riboflavin biosynthetic process
Components
  • cytosol
General FunctionRiboflavin synthase activity
Specific FunctionCatalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil.
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP0AFU8
UniProtKB Entry Name
Cellular LocationNone
Gene sequence
>lcl|BSEQ0012327|Riboflavin synthase (ribC)
ATGTTTACGGGGATTGTACAGGGCACCGCAAAACTGGTGTCGATTGACGAGAAACCAAAT
TTTCGTACGCATGTGGTGGAGTTACCCGACCACATGCTGGACGGCCTGGAAACCGGTGCT
TCCGTGGCGCATAACGGTTGCTGCCTGACCGTGACGGAAATTAACGGCAACCATGTCAGT
TTTGACCTGATGAAAGAAACGTTACGCATTACCAATCTTGGCGATTTAAAAGTGGGGGAT
TGGGTAAACGTTGAGCGTGCGGCGAAATTCAGTGATGAAATTGGCGGACACTTAATGTCA
GGTCATATTATGACCACTGCTGAAGTGGCGAAAATATTAACCTCAGAAAATAATCGCCAG
ATCTGGTTTAAAGTCCAGGATAGTCAGTTGATGAAATATATTCTGTACAAAGGATTTATT
GGCATCGACGGTATTAGCCTGACCGTCGGCGAAGTCACGCCAACGCGTTTTTGCGTCCAT
TTAATTCCGGAAACACTGGAACGCACGACTCTTGGGAAGAAAAAACTTGGCGCACGCGTC
AACATTGAAATCGATCCACAAACTCAGGCAGTGGTAGATACGGTAGAACGTGTGCTGGCG
GCACGAGAAAATGCCATGAATCAACCAGGCACAGAAGCCTGA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. 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. [9022701 ]
  2. 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. [9023191 ]
  3. 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. [9097039 ]
  4. 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. [9278503 ]
  5. 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. [16738553 ]
  6. 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. [11399071 ]
  7. Liao DI, Wawrzak Z, Calabrese JC, Viitanen PV, Jordan DB: Crystal structure of riboflavin synthase. Structure. 2001 May 9;9(5):399-408. [11377200 ]
  8. 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. [12927541 ]

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