6,7-dimethyl-8-ribityllumazine synthase

Details

Name
6,7-dimethyl-8-ribityllumazine synthase
Synonyms
  • 2.5.1.78
  • DMRL synthase
Gene Name
ribH
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Amino acid sequence
>lcl|BSEQ0051159|6,7-dimethyl-8-ribityllumazine synthase
MKGGAGVPDLPSLDASGVRLAIVASSWHGKICDALLDGARKVAAGCGLDDPTVVRVLGAI
EIPVVAQELARNHDAVVALGVVIRGQTPHFDYVCDAVTQGLTRVSLDSSTPIANGVLTTN
TEEQALDRAGLPTSAEDKGAQATVAALATALTLRELRAHS
Number of residues
160
Molecular Weight
16370.415
Theoretical pI
Not Available
GO Classification
Functions
6,7-dimethyl-8-ribityllumazine synthase activity / transferase activity
Processes
growth / riboflavin biosynthetic process
Components
cytosol / riboflavin synthase complex
General Function
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Specific Function
6,7-dimethyl-8-ribityllumazine synthase activity
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0051160|6,7-dimethyl-8-ribityllumazine synthase (ribH)
GTGAAGGGTGGCGCCGGGGTGCCGGATCTGCCGTCGCTGGATGCGTCTGGTGTGCGGCTG
GCGATTGTCGCCAGCAGCTGGCACGGAAAGATCTGCGACGCGCTGTTGGACGGCGCCCGC
AAGGTGGCCGCCGGGTGTGGCCTCGATGACCCGACTGTGGTTCGGGTGCTCGGCGCGATC
GAGATTCCGGTGGTGGCGCAGGAATTGGCCCGCAATCATGATGCCGTCGTCGCACTTGGC
GTCGTGATCCGCGGTCAGACACCACATTTCGACTACGTGTGCGATGCGGTAACCCAGGGA
CTGACCCGGGTATCGCTGGATTCCTCGACGCCGATCGCCAACGGCGTGCTGACCACCAAC
ACCGAGGAGCAGGCGCTGGATCGGGCGGGGCTACCGACGTCGGCCGAGGACAAGGGCGCC
CAGGCGACTGTGGCAGCCCTGGCCACCGCGTTGACCCTGCGCGAGCTGCGCGCTCACTCG
TGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP9WHE9
UniProtKB Entry NameRISB_MYCTU
General References
  1. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
  2. Cushman M, Sambaiah T, Jin G, Illarionov B, Fischer M, Bacher A: Design, synthesis, and evaluation of 9-D-ribitylamino-1,3,7,9-tetrahydro-2,6,8-purinetriones bearing alkyl phosphate and alpha,alpha-difluorophosphonate substituents as inhibitors of tiboflavin synthase and lumazine synthase. J Org Chem. 2004 Feb 6;69(3):601-12. [Article]
  3. Rison SC, Mattow J, Jungblut PR, Stoker NG: Experimental determination of translational starts using peptide mass mapping and tandem mass spectrometry within the proteome of Mycobacterium tuberculosis. Microbiology. 2007 Feb;153(Pt 2):521-8. [Article]
  4. Raman K, Yeturu K, Chandra N: targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis. BMC Syst Biol. 2008 Dec 19;2:109. doi: 10.1186/1752-0509-2-109. [Article]
  5. Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [Article]
  6. Morgunova E, Meining W, Illarionov B, Haase I, Jin G, Bacher A, Cushman M, Fischer M, Ladenstein R: Crystal structure of lumazine synthase from Mycobacterium tuberculosis as a target for rational drug design: binding mode of a new class of purinetrione inhibitors. Biochemistry. 2005 Mar 1;44(8):2746-58. [Article]
  7. Morgunova E, Illarionov B, Sambaiah T, Haase I, Bacher A, Cushman M, Fischer M, Ladenstein R: Structural and thermodynamic insights into the binding mode of five novel inhibitors of lumazine synthase from Mycobacterium tuberculosis. FEBS J. 2006 Oct;273(20):4790-804. Epub 2006 Sep 19. [Article]
  8. Zhang Y, Illarionov B, Morgunova E, Jin G, Bacher A, Fischer M, Ladenstein R, Cushman M: A new series of N-[2,4-dioxo-6-d-ribitylamino-1,2,3,4-tetrahydropyrimidin-5-yl]oxalamic acid derivatives as inhibitors of lumazine synthase and riboflavin synthase: design, synthesis, biochemical evaluation, crystallography, and mechanistic implications. J Org Chem. 2008 Apr 4;73(7):2715-24. doi: 10.1021/jo702631a. Epub 2008 Mar 11. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01692DithioerythritolexperimentalunknownDetails
DB021351-deoxy-1-{2,6,8-trioxo-7-[4-(phosphonooxy)butyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl}-D-arabinitolexperimentalunknownDetails
DB02184D-1,4-dithiothreitolexperimentalunknownDetails
DB022903-{2,6,8-trioxo-9-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,6,8,9-hexahydro-7H-purin-7-Yl}propyl dihydrogen phosphateexperimentalunknownDetails
DB02693(4S,5S)-1,2-dithiane-4,5-diolexperimentalunknownDetails
DB027114-{2,6,8-Trioxo-9-[(2S,3R,4R)-2,3,4,5-Tetrahydroxypentyl]-1,2,3,6,8,9-Hexahydro-7h-Purin-7-Yl}Butyl Dihydrogen PhosphateexperimentalunknownDetails
DB030223-[2,6,8-Trioxo-9-[(2R,3S,4R)-2,3,4,5-tetrahydroxypentyl]-3H-purin-7-yl]propyl dihydrogen phosphateexperimentalunknownDetails
DB038123-{2,6,8-trioxo-9-[(2S,3R,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,6,8,9-hexahydro-7H-purin-7-Yl}propyl dihydrogen phosphateexperimentalunknownDetails
DB039733-[2,6,8-Trioxo-9-[(2R,3R,4R)-2,3,4,5-tetrahydroxypentyl]-3H-purin-7-yl]propyl dihydrogen phosphateexperimentalunknownDetails
DB080164-(6-CHLORO-2,4-DIOXO-1,2,3,4-TETRAHYDROPYRIMIDIN-5-YL) BUTYL PHOSPHATEexperimentalunknownDetails