Abstract
Here, we report the draft annotated genome sequence of Streptomyces mobaraensis strain DSM 40847, which is used in industry to produce microbial transglutaminase. The genome sequence will allow for the characterization of the molecular mechanisms underlying the beneficial properties of this organism.
Highlights
We report the draft annotated genome sequence of Streptomyces mobaraensis strain DSM 40847, which is used in industry to produce microbial transglutaminase
TGases derived from eukaryotes, including human blood coagulation factor XIII [2], human tissue TG [2], pig liver TG [3], and fish liver TG [4], are calcium-dependent, polysubunit enzymes
There are nine distinct TG isoenzymes in mammals that have been identified at the genomic level, of which eight are structurally and functionally related to the function of TGases, viz., TG 1 to 7 and factor XIII [5, 6]
Summary
We report the draft annotated genome sequence of Streptomyces mobaraensis strain DSM 40847, which is used in industry to produce microbial transglutaminase. Transglutaminases (TGases) (protein-glutamine ␥-glutamyltransferases, EC 2.3.2.13) are a family of enzymes that catalyze an acyl transfer reaction between a free amine group and a ␥-carboximide group of protein-bound or peptide-bound glutamine [1]. TGases derived from eukaryotes, including human blood coagulation factor XIII [2], human tissue TG [2], pig liver TG [3], and fish liver TG [4], are calcium-dependent, polysubunit enzymes. There are nine distinct TG isoenzymes in mammals that have been identified at the genomic level, of which eight are structurally and functionally related to the function of TGases, viz., TG 1 to 7 and factor XIII [5, 6]. Calcium-independent TGases with only one subunit have been discovered in Streptomyces [7] and Bacillus [8].
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