Genomic loci for this biosynthetic pathway

Cluster Type From To
The following clusters are from record BGC0000384.1:
Cluster 1NRP117000

BGC0000384, lyngbyatoxin biosynthetic gene cluster from Lyngbya majuscula. Locus 1. Full MIBiG entry.

Chemical compounds

Compound: Lyngbyatoxin
PubChem ID: 91706
ChEBI ID: 80050
ChemSpider ID: 10472344
SMILES string: Copy to clipboard
Molecular formula: C27H39N3O2
Average molecular mass: 437.628 Da
Molecular activity: Cytotoxic, Other
Molecular target: Protein kinase C (activator)

Class-specific details

Biosynthetic class(es):
Other (cyclic)
Thioesterase type:
Release / cyclization type:
Reductive release

Nonribosomal peptide synthetases:
ltxA (AAT12283)
Module 2
A specificity: Tryptophan
Evidence for specificity: Structure-based inference
C domain subtype: LCL
Module 1
A specificity: Valine
Evidence for specificity: Structure-based inference
C domain subtype: Other
Scaffold-modifying domain: Methylation

Gene cluster description

lyngbyatoxin (BGC0000384). Gene Cluster 1. Biosynthetic class = NRP. GenBank AY588942, positions 2740-13999. Click on genes for more information.


biosynthetic genes
transport-related genes
regulatory genes
other genes

Domain annotation

Homologous known gene clusters

General MIBiG information on this cluster

Complete gene cluster sequence?complete
Evidence for cluster-compound connection:Enzymatic assays, Heterologous expression, Sequence-based prediction
Comments:Only one condensation domain is present within AAT12283
Contact for this cluster:Adam Jones (Fairfax, VA USA)

Literature references

1. Cardellina JH 2nd et al. (1979) Seaweed dermatitis: structure of lyngbyatoxin A. Science 204(4389):193-5.
2. Edwards DJ, Gerwick WH. (2004) Lyngbyatoxin biosynthesis: sequence of biosynthetic gene cluster and identification of a novel aromatic prenyltransferase. J Am Chem Soc 126(37):11432-3. doi: 10.1021/ja047876g.
3. Huynh MU et al. (2010) Enzymatic production of (-)-indolactam V by LtxB, a cytochrome P450 monooxygenase. J Nat Prod 73(1):71-4. doi: 10.1021/np900481a.
4. Jones AC et al. (2012) Evaluation of Streptomyces coelicolor A3(2) as a heterologous expression host for the cyanobacterial protein kinase C activator lyngbyatoxin A. FEBS J 279(7):1243-51. doi: 10.1111/j.1742-4658.2012.08517.x. Epub 2012
5. CODOUNIS A. (1962) [Remote results of splenectomy for Mediter-ranean erythroblastic anemia]. Rev Med Moyen Orient 19:51-7.
6. Nathel NF et al. (2014) Total syntheses of indolactam alkaloids (-)-indolactam V, (-)-pendolmycin, (-)-lyngbyatoxin A, and (-)-teleocidin A-2. Chem Sci 5(6):2184-2190. doi: 10.1039/C4SC00256C.
7. Ongley SE et al. (2013) High-titer heterologous production in E. coli of lyngbyatoxin, a protein kinase C activator from an uncultured marine cyanobacterium. ACS Chem Biol 8(9):1888-93. doi: 10.1021/cb400189j. Epub 2013 Jun