Functional, and phylogenetic analysis of maleylacetate reductase of Pseudomonas sp strain PNPG3: An in-silico approach

Sk Aftabul Alam; Pradipta Saha

doi:10.18006/2022.10(6).1331.1343

Authors

Sk Aftabul Alam Department of Microbiology, The University of Burdwan, Golapbag, Burdwan-713104, WB, India https://orcid.org/0000-0002-6668-4383
Pradipta Saha Department of Microbiology, The University of Burdwan, Golapbag, Burdwan-713104, WB, India https://orcid.org/0000-0003-2113-3198

DOI:

https://doi.org/10.18006/2022.10(6).1331.1343

Keywords:

Maleylacetate reductase, Pseudomonas, PNP biodegradation, Homology modeling, STRING database

Abstract

Shrinking freshwater ecosystems are under tremendous pollution threat due to anthropocentric activities. Para nitrophenol (PNP), a well-documented priority pollutant extensively used in dyes, petrochemical, pharmaceutical, explosives, pesticides, leather industries, and agrochemicals, is responsible for contaminating aquatic ecosystems globally. It is highly toxic and has carcinogenic and mutagenic effects on living organisms like humans and several animal models. Bioremediation approaches mainly involving bacteria are considered the best, most eco-friendly, cost-effective, green, and clean method for effective removal PNP from its contaminated sites. This manuscript highlights the structural and functional analysis of a lower pathway enzyme involved in PNP degradation, maleylacetate reductase (MR), from Pseudomonas sp strain PNPG3, which was recently isolated from a freshwater ecosystem. This enzyme plays a role in converting maleylacetate to 3-oxoadipate. Despite its crucial functional role, no model is available for this protein in the protein database (PDB). Therefore, attempts were made for the computational investigation of physicochemical, functional, and structural properties, including secondary, and tertiary structure prediction, model quality analysis, and phylogenetic assessment using several standard bioinformatics tools. This enzyme has a molecular weight of about ~37.6 kDa, is acidic and thermostable, belonging to a member of iron-containing alcohol dehydrogenase. Moreover, this study will benefit the scientific community in deciphering the prediction of the function of similar proteins of interest.

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