Genomic loci for this biosynthetic pathway

Cluster Type From To
The following clusters are from record BGC0000297.1:
Cluster 1NRP / Polyketide / Saccharide131449

BGC0000297, aeruginoside biosynthetic gene cluster from Planktothrix agardhii. Locus 1. Full MIBiG entry.

Chemical compounds

Compound: Aeruginoside 126B
SMILES string: Copy to clipboard
Molecular formula: C34H53N6O9
Exact molecular mass: 691.4051 Da ([M+H]+)
Molecular activity: Unknown

Class-specific details

Biosynthetic class(es):
NRP / Polyketide / Saccharide
Glycopeptide (linear)
Thioesterase type:
Release / cyclization type:

Nonribosomal peptide synthetases:
aerA (CAM59601.1)
Module 0
A specificity: Unknown
Evidence for specificity: Unknown
Scaffold-modifying domain: Other
aerB (CAJ21198.2)
Module 1
A specificity: Leucine
Evidence for specificity: Sequence-based prediction
AA is epimerized
C domain subtype: LCL
aerG (CAM59606.1)
Module 2
A specificity: 2-carboxy-6-hydroxy-octahydroindole
Evidence for specificity: Unknown
Amino acid biosynthesis subcluster: caj21199.2,cam59603.1,cam59604.1,cam59605.1
C domain subtype: DCL
Polyketide subclass:
Other (linear)
Polyketide synthase subclass:
Starter unit:
Polyketide synthase / ketosynthase-encoding genes:

Gene cluster description

aeruginoside (BGC0000297). Gene Cluster 1. Biosynthetic class = NRP/Polyketide/Saccharide. GenBank AM071396, positions 2649-24685. 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:Knock-out studies, Enzymatic assays, Sequence-based prediction
Contact for this cluster:Keishi Ishida (Leipniz Institute for Natural Product Research and Infection Biology)

Literature references

1. Ishida K et al. (2007) Biosynthesis and structure of aeruginoside 126A and 126B, cyanobacterial peptide glycosides bearing a 2-carboxy-6-hydroxyoctahydroindole moiety. Chem Biol 14(5):565-576. doi: 10.1016/j.chembiol.2007.04.006.
2. Mahlstedt S et al. (2010) Prephenate decarboxylases: a new prephenate-utilizing enzyme family that performs nonaromatizing decarboxylation en route to diverse secondary metabolites. Biochemistry 49(42):9021-3. doi: 10.1021/bi101457h.
3. Ishida K et al. (2009) Plasticity and evolution of aeruginosin biosynthesis in cyanobacteria. Appl Environ Microbiol 75(7):2017-26. doi: 10.1128/AEM.02258-08. Epub