The metagenomic is a powerful method to study this search soil. Upon screening 10,000 clones, each one carrying recombinant cosmid exhibited inorganic pyrophosphatase (PPase, EC 3.6.1.1) and thioesterase protein. The PPase is an essential enzyme catalyzing the cation-dependent interconversion of inorganic pyrophosphate and orthophosphate. This reaction provides a thermodynamic pull for many biosynthetic reactions. The recent application the PPase is an additive in animal feeds and in the textile industry. The Bioinformatics is a step forward in proteomics of protein method appears as a strategy of choice to generate in silico hypotheses for experimental testing. The sequence of the protein 3D structure was predicted using the I-Tasser server. We can see (Fig.1) PPase (A) protein structure prediction using the I-Tasser server the image (B) is a picture of the model constructed for your sequence based on that template. We considering that this is a new PPase as given below have been modelled with 100.0% confidence by the single highest scoring template is a true homology, code template PDB 4A01, i.d. was of 25%, Fold: H_PPase, Superfamily:  H(+)-translocating pyrophosphatase. With these specials features on this PPase will perform cloning in vector pET28a; our results suggest that these characteristics obtained for this enzyme will further contribute to heterologous expression assays. The thioester hydrolases or thioesterases (TEs) comprise a large enzyme group whose members hydrolyze the thioester bond between a carbonyl group and a sulfur atom. The recent application of TEs is the overproduction of biodiesel from fatty acids using microbial thioesterases. The Bioinformatics is a step forward in proteomics of protein method appears as a strategy of choice to generate in silico hypotheses for experimental testing. The sequence of the protein for which the 3D structure was predicted using the Phyre server. Can see (Fig.2) thioesterase (A) protein structure prediction using the Phyre server the image (B) is a picture of the model constructed for your sequence based on that template. We considering that this is a new thioesterase as given below have been modelled with 100.0% confidence by the single highest scoring template is a true homology, code template d2nuja1, i.d. was of 25%, Fold: Thioesterase/thiol ester dehydrase-isomerase, Superfamily: Thioesterase/thiol ester dehydrase-isomerase, Family: 4HBT-like. Which suggests that special features on these results in situ for future us cloning into the expression vector pET 28b

Figure 1: Constructing 3D models of our protein based on the alignments between the HMM of your sequence and the HMMs of known structure where A) PPase metagenomic and B) Template was code PDB 4A01.

Figure 2: Constructing 3D models of our protein based on the alignments between the HMM of your sequence and the HMMs of known structure where A) is thioesterase metagenomic and B) is template.

Keywords: Thioester hydrolases, biotechnology, crystallization, PPase, superfamily