(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 > Streptomycetales: NE > Streptomycetaceae: NE > Streptomyces: NE > unclassified Streptomyces: NE > Streptomyces sp. OM5714: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide 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.) Streptomyces coelicoflavus ZG0656: N, E.
Streptomyces sp. CS159: 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 MRKVVSRDGTTIAYEKTGDGPPIVLLNGSFRDHTIFDALVPELAPHCTTY VYDRRGRGQSGDSPEYAVGREIEDLEAVIQEAGGSAVVFAGSSGANLAVE AALAGAPISKLALHEPFYRVDGFPKPPWNVAKTLRVLMAEDRREEAVEYY LGSFLGLTPDTVAQWRQGPIWAVNEANAHTLAYDLAICGDCTVPAERLAG YTTQTLVLNSSGTSEWLRAAARATAAALPEGRSLELPGSWHRIDMDVLGR TLAEFATA
References
Title: Identification of Alp1U and Lom6 as epoxy hydrolases and implications for kinamycin and lomaiviticin biosynthesis Wang B, Guo F, Ren J, Ai G, Aigle B, Fan K, Yang K Ref: Nat Commun, 6:7674, 2015 : PubMed
The naturally occurring diazobenzofluorenes, kinamycins, fluostatins and lomaiviticins, possess highly oxygenated A-rings, via which the last forms a dimeric pharmacophore. However, neither the A-ring transformation nor the dimerization mechanisms have been explored thus far. Here we propose a unified biosynthetic logic for the three types of antibiotics and verify one key reaction via detailed genetic and enzymatic experiments. Alp1U and Lom6 from the kinamycin and lomaiviticin biosynthesis, respectively, are shown to catalyse epoxy hydrolysis on a substrate that is obtained by chemical deacetylation of a kinamycin-pathway-derived intermediate. Thus, our study provides the first evidence for the existence of an epoxy intermediate in lomaiviticin biosynthesis. Furthermore, our results suggest that the dimerization in the lomaiviticin biosynthesis proceeds after dehydration of a product generated by Lom6.
Title: Draft genome sequence of Streptomyces coelicoflavus ZG0656 reveals the putative biosynthetic gene cluster of acarviostatin family alpha-amylase inhibitors Guo X, Geng P, Bai F, Bai G, Sun T, Li X, Shi L, Zhong Q Ref: Lett Appl Microbiol, 55:162, 2012 : PubMed
AIMS: The aims of this study are to obtain the draft genome sequence of Streptomyces coelicoflavus ZG0656, which produces novel acarviostatin family alpha-amylase inhibitors, and then to reveal the putative acarviostatin-related gene cluster and the biosynthetic pathway. METHODS AND RESULTS: The draft genome sequence of S. coelicoflavus ZG0656 was generated using a shotgun approach employing a combination of 454 and Solexa sequencing technologies. Genome analysis revealed a putative gene cluster for acarviostatin biosynthesis, termed sct-cluster. The cluster contains 13 acarviostatin synthetic genes, six transporter genes, four starch degrading or transglycosylation enzyme genes and two regulator genes. On the basis of bioinformatic analysis, we proposed a putative biosynthetic pathway of acarviostatins. The intracellular steps produce a structural core, acarviostatin I00-7-P, and the extracellular assemblies lead to diverse acarviostatin end products. CONCLUSIONS: The draft genome sequence of S. coelicoflavus ZG0656 revealed the putative biosynthetic gene cluster of acarviostatins and a putative pathway of acarviostatin production. SIGNIFICANCE AND IMPACT OF THE STUDY: To our knowledge, S. coelicoflavus ZG0656 is the first strain in this species for which a genome sequence has been reported. The analysis of sct-cluster provided important insights into the biosynthesis of acarviostatins. This work will be a platform for producing novel variants and yield improvement.
