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Description: Summary: Background: The microbial enzyme hydrogenase form hydrogen by catalysing the chemical reaction (8), and play a central role in microbial energy metabolism, maintaining ozone layer around the earth, help to combat with diseases like liver diseases, GI tract diseases, and used as bio-fuel -for electricity generation and biosensor for various biological reactions. Although its structural characteristics have yet to be determined and the data presented have been close in proximity to predict the three dimensional structure of enzyme, membrane and nuclear protein of the bacteria. The enzymes producing bacteria belong to Archaea and anaerobes like Clostridium spp., Desulfovibri spp. (9) and cyanobacteria and aerobes like green algae chloroplast, but not in animal eukaryotic cells. The widespread classes of Proteobacteria, as well as Firmicutes, Cyanobacteria, Aquificae, Euryarchaeota and Crenarchaeota produce hydrogenase and present on the surface of fresh water and marine ecosystem (5) for example in North Atlantic, Mediterranean Sea, North Sea, the Baltic Sea and the fresh water lakes Westensee and Selenter Sea in Northern Germany. My Approach: The presence of genebank (http://www.ncbi.nlm.nih.gov/) and cyanobase (http://bacteria.kazusa.or.jp/cyanobase/) help for sequence alignment for other hydrogenase for structural analysis. The bacterial species of Anabaena variabilis, Microcystis aeruginosa, Nostoc, Prochlorothrix hollandica, Gloeocapsa alpicola and Arthrospira maxima are the fresh water Hydrogenase enzyme producing bacteria. Mycobacterium marinum and Rhodococcus erthropolis of the class Actinobacteria and Flavobacteia bacterium, Prosthecochloris aestuarii and Robiginitalea biformata of the class Bacteroidetes (7), show similarity in functional algorythms and will align for their sequence to model their gene and enzyme. Goal: The goal of the study is to retrieve data to identify the structural homolog. The data will be mined from the survey on web science.gov, CORE, semantic scholar, RefSeek, scienceopen, the lens, citation gecko, local citation network, researchrabbit, open access button, NIH Pubmed, genebank. The target–template alignment on tools like BLAST, FASTA, UNIPROT, The Swiss-PdbViewer (http://www.expasy.ch/spdbv/mainpage.html), and model building and optimization, and model evaluation by (http://www.expasy.ch/swissmod/SWISS-MODEL.html) and ESyPred3D (http://www.fundp.ac.be/urbm/bioinfo/esypred/) (4, 6, 8). We present our result of model in an App designed digitally on web. REFERENCES: 1. Zubaida Khatoon and RK Kale, Radiomodulation by Hoechst 33258 against radiation- induced damage in murine splenocytes, Indian Journal of Experimental Biology, 2012, vol.50, 517-530. 2. Radiomodulation by Bibenzimidazole, Z. Khatoon, R. K. Kale. Shodhganga:a reservoir of indian theses @ inflibnet. 3. Radiomodulation by Bibenzimidazole, Z. Khatoon, R. K. Kale. Annual Report ICMR Headquarters 2005-2006, Noncommunicable Diseases, pg 118 (ICMR India for Senor Research Fellowship). 4. Diemand A, Manuel C, Show Pmore, Protein modelling for all, Trends In Biochemical Sciences, 199, vol. 24 (9), 264-367. 5. Lappan R, Shelley G, Islam FZ, Pok Man Leung PK et. al, Molecular hydrogen in seawater supports growth of diverse marine bacteria, Nature Microbiology, 2023, vol. 8, 581-595. 6. Silva MB, Buriol SL, Luis C. Lamb CL, Three-dimensional protein structure prediction: Methods and computational strategies, Computational Biology and Chemistry, 2014, 251-276. 7. Barz M, Beimgraben C, Staller T, Germer F,. et. al. Distribution Analysis of Hydrogenases in Surface Waters of Marine and Freshwater Environments, 2012, PloS One, Vol. 5(11) e13846. 8. Wu HC, Haja KD, Adams WWM., Chapter Six - Cytoplasmic and membrane-bound hydrogenases from Pyrococcus furiosus, Methods in Enzymology, 2018, vol. 613, 153-168. 9. Pohorelic BKJ, Voordouw JK, Lojou E, Dolla A, Harder J, Voordouw G2002.Effects of Deletion of Genes Encoding Fe-Only Hydrogenase of Desulfovibrio vulgaris Hildenborough on Hydrogen and Lactate Metabolism. J Bacteriol184:.https://doi.org/10.1128/jb.184.3.679-686.2002.