(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Terrabacteria group: NE > Actinobacteria [phylum]: NE > Actinobacteria [class]: NE > Micromonosporales: NE > Micromonosporaceae: NE > Verrucosispora: NE > Verrucosispora maris: NE > Verrucosispora maris AB-18-032: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acid identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Verrucosispora maris AB-18-032: N, E.
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MSNDVAELKQYVLAHVSAQNASADGVLARIDDDGDGPRSWTTQWIRAGEE REQAGDLLAATTFYNLARFPFVDSPGRAEALRRCVAVFDRWRRTVPGIER LELRLPGGVVRAWAAGLSTTERRPVLLMTGGIVSIKEQWAPILPELARYG FAAVVTELPGVGENELRYDLDSAALFGVLLDAVAERADTSRAYALALSFS GHLALRAAPSEPRLRGIVTAGAPVAAFFTDKEWQAAVPRVTVDTLARLTQ TTPATVFDHVRNWALTPQDLAGVRIPVAYVASGRDEIIPPADPALLRTHV RDFRTITHDDVHGSPAHFPHTRLWTLAQVLEMSGADPRHRAAVDGALAQV EGGRA
Spirotetronate and spirotetramate natural products include a multitude of compounds with potent antimicrobial and antitumor activities. Their biosynthesis incorporates many unusual biocatalytic steps, including regio- and stereo-specific modifications, cyclizations promoted by Diels-Alderases, and acetylation-elimination reactions. Here we focus on the acetate elimination catalyzed by AbyA5, implicated in the formation of the key Diels-Alder substrate to give the spirocyclic system of the antibiotic abyssomicin C. Using synthetic substrate analogues, it is shown that AbyA5 catalyzes stereospecific acetate elimination, establishing the (R)-tetronate acetate as a biosynthetic intermediate. The X-ray crystal structure of AbyA5, the first of an acetate-eliminating enzyme, reveals a deviant acetyl esterase fold. Molecular dynamics simulations and enzyme assays show the use of a His-Ser dyad to catalyze either elimination or hydrolysis, via disparate mechanisms, under substrate control.
Verrucosispora maris (strain AB-18-032) AbyA5
