6,7-dimethyl-8-ribityllumazine synthase

Details

Name
6,7-dimethyl-8-ribityllumazine synthase
Kind
protein
Synonyms
  • 2.5.1.78
  • DMRL synthase
Gene Name
ribH
UniProtKB Entry
O66529Swiss-Prot
Organism
Aquifex aeolicus (strain VF5)
NCBI Taxonomy ID
224324
Amino acid sequence
>lcl|BSEQ0011018|6,7-dimethyl-8-ribityllumazine synthase
MQIYEGKLTAEGLRFGIVASRFNHALVDRLVEGAIDCIVRHGGREEDITLVRVPGSWEIP
VAAGELARKEDIDAVIAIGVLIRGATPHFDYIASEVSKGLANLSLELRKPITFGVITADT
LEQAIERAGTKHGNKGWEAALSAIEMANLFKSLR
Number of residues
154
Molecular Weight
16705.035
Theoretical pI
6.11
GO Classification
Functions
6,7-dimethyl-8-ribityllumazine synthase activity / transferase activity
Processes
riboflavin biosynthetic process
Components
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
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011019|6,7-dimethyl-8-ribityllumazine synthase (ribH)
ATGCAAATTTACGAAGGGAAACTAACCGCTGAAGGGCTGAGGTTCGGTATAGTGGCTTCC
AGGTTCAACCACGCACTCGTGGATAGACTAGTTGAGGGAGCTATAGACTGCATAGTAAGA
CACGGGGGAAGGGAAGAAGACATAACGCTCGTTAGAGTGCCGGGCTCCTGGGAAATTCCC
GTGGCTGCGGGAGAGCTTGCGAGAAAAGAGGACATAGACGCTGTGATAGCGATAGGAGTT
CTAATAAGGGGGGCTACTCCCCACTTTGATTACATAGCCTCTGAAGTGTCAAAAGGGCTT
GCGAACCTTTCCTTAGAACTGAGAAAACCCATAACCTTCGGTGTTATAACTGCGGACACC
TTGGAGCAGGCGATAGAAAGGGCGGGAACAAAGCACGGGAATAAGGGCTGGGAAGCTGCA
CTTTCCGCAATAGAAATGGCAAACTTATTTAAGAGTCTGAGATGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDO66529
UniProtKB Entry NameRISB_AQUAE
GenBank Protein ID2982869
GenBank Gene IDAE000657
PDB ID(s)1HQK, 1NQU, 1NQV, 1NQW, 1NQX
KEGG IDaae:aq_132
NCBI Gene ID1192672
General References
  1. Deckert G, Warren PV, Gaasterland T, Young WG, Lenox AL, Graham DE, Overbeek R, Snead MA, Keller M, Aujay M, Huber R, Feldman RA, Short JM, Olsen GJ, Swanson RV: The complete genome of the hyperthermophilic bacterium Aquifex aeolicus. Nature. 1998 Mar 26;392(6674):353-8. [Article]
  2. Haase I, Mortl S, Kohler P, Bacher A, Fischer M: Biosynthesis of riboflavin in archaea. 6,7-dimethyl-8-ribityllumazine synthase of Methanococcus jannaschii. Eur J Biochem. 2003 Mar;270(5):1025-32. [Article]
  3. Zhang X, Meining W, Fischer M, Bacher A, Ladenstein R: X-ray structure analysis and crystallographic refinement of lumazine synthase from the hyperthermophile Aquifex aeolicus at 1.6 A resolution: determinants of thermostability revealed from structural comparisons. J Mol Biol. 2001 Mar 9;306(5):1099-114. [Article]
  4. Zhang X, Meining W, Cushman M, Haase I, Fischer M, Bacher A, Ladenstein R: A structure-based model of the reaction catalyzed by lumazine synthase from Aquifex aeolicus. J Mol Biol. 2003 Apr 18;328(1):167-82. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
6,7-dioxo-5H-8-ribitylaminolumazineexperimentalunknowntargetDetails
5-Nitroso-6-ribityl-amino-2,4(1H,3H)-pyrimidinedioneexperimentalunknowntargetDetails
3-(7-hydroxy-8-ribityllumazine-6-yl) propionic acidexperimentalunknowntargetDetails