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Pathway Description
Flavin Biosynthesis
Escherichia coli 536
Category:
Metabolite Pathway
Sub-Category:
Metabolic
Created: 2025-02-03
Last Updated: 2025-02-03
The process of flavin biosynthesis starts with GTP being metabolized by interacting with 3 molecules of water through a GTP cyclohydrolase resulting in a release of formic acid, a pyrophosphate, two hydrog ions and 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one or 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine. Either of these compounds interacts with a water molecule and a hydrogen ion through a fused diaminohydroxyphosphoribosylaminopyrimidine deaminase / 5-amino-6-(5-phosphoribosylamino)uracil reductase resulting in an ammonium and 5-amino-6-(5-phospho-D-ribosylamino)uracil. This compound then interacts with a hydrogen ion through a NADPH dependent fused diaminohydroxyphosphoribosylaminopyrimidine deaminase / 5-amino-6-(5-phosphoribosylamino)uracil reductase resulting in the release of a NADP and a 5-amino-6-(5-phospho-D-ribitylamino)uracil. This compound then interacts with a water molecule through a 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase resulting in a release of a phosphate, and a 5-amino-6-(D-ribitylamino)uracil.
D-ribulose 5-phosphate interacts with a3,4-dihydroxy-2-butanone 4-phosphate synthase resulting in the release of formic acid, a hydrogen ion and 1-deoxy-L-glycero-tetrulose 4-phosphate.
A 5-amino-6-(D-ribitylamino)uracil and 1-deoxy-L-glycero-tetrulose 4-phosphate interact through a 6,7-dimethyl-8-ribityllumazine synthase resulting in the release of 2 water molecules, a phosphate, a hydrogen ion and a 6,7-dimethyl-8-(1-D-ribityl)lumazine.
The latter compound then interacts with a hydrogen ion through a riboflavin synthase resulting in the release of a riboflavin and a 5-amino-6-(d-ribitylamino)uracil.
The riboflavin is then phosphorylated through an ATP dependent riboflavin kinase resulting in the release of a ADP, a hydrogen ion and a FLAVIN MONONUCLEOTIDE.
The flavin mononucleotide interad with a hydrogen ion and an ATP through the riboflavin kinase resulting in the release of a pyrophosphate and Flavin Adenine dinucleotide. This compound is then exported into the periplasm through a FMN/FAD exporter.
References
Flavin Biosynthesis References
Katzenmeier G, Schmid C, Kellermann J, Lottspeich F, Bacher A: Biosynthesis of tetrahydrofolate. Sequence of GTP cyclohydrolase I from Escherichia coli. Biol Chem Hoppe Seyler. 1991 Nov;372(11):991-7.
Pubmed: 1665332
Schmid C, Meining W, Weinkauf S, Bachmann L, Ritz H, Eberhardt S, Gimbel W, Werner T, Lahm HW, Nar H, et al.: Studies on GTP cyclohydrolase I of Escherichia coli. Adv Exp Med Biol. 1993;338:157-62. doi: 10.1007/978-1-4615-2960-6_30.
Pubmed: 8304099
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. doi: 10.1126/science.277.5331.1453.
Pubmed: 9278503
Taura T, Ueguchi C, Shiba K, Ito K: Insertional disruption of the nusB (ssyB) gene leads to cold-sensitive growth of Escherichia coli and suppression of the secY24 mutation. Mol Gen Genet. 1992 Sep;234(3):429-32. doi: 10.1007/bf00538702.
Pubmed: 1406588
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. doi: 10.1038/msb4100049. Epub 2006 Feb 21.
Pubmed: 16738553
Colloms SD, Sykora P, Szatmari G, Sherratt DJ: Recombination at ColE1 cer requires the Escherichia coli xerC gene product, a member of the lambda integrase family of site-specific recombinases. J Bacteriol. 1990 Dec;172(12):6973-80. doi: 10.1128/jb.172.12.6973-6980.1990.
Pubmed: 2254268
Daniels DL, Plunkett G 3rd, Burland V, Blattner FR: Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes. Science. 1992 Aug 7;257(5071):771-8. doi: 10.1126/science.1379743.
Pubmed: 1379743
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. doi: 10.1111/j.1432-1033.1996.0712r.x.
Pubmed: 9022701
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. doi: 10.1128/jb.179.4.1105-1111.1997.
Pubmed: 9023191
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. doi: 10.1093/dnares/3.6.363.
Pubmed: 9097039
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. doi: 10.1016/s0022-2836(03)00844-1.
Pubmed: 12927541
Kamio Y, Lin CK, Regue M, Wu HC: Characterization of the ileS-lsp operon in Escherichia coli. Identification of an open reading frame upstream of the ileS gene and potential promoter(s) for the ileS-lsp operon. J Biol Chem. 1985 May 10;260(9):5616-20.
Pubmed: 2985604
Yura T, Mori H, Nagai H, Nagata T, Ishihama A, Fujita N, Isono K, Mizobuchi K, Nakata A: Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region. Nucleic Acids Res. 1992 Jul 11;20(13):3305-8. doi: 10.1093/nar/20.13.3305.
Pubmed: 1630901
This pathway was propagated using PathWhiz -
Pon, A. et al. Pathways with PathWhiz (2015) Nucleic Acids Res. 43(Web Server issue): W552–W559.
Propagated from SMP0001985
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