IN SILICO ANALYSIS OF A PUTATIVE MOLYBDENUM TRANSPORTER (MoT) IN BUFFALO

Almost all living organism require to transport molybdenum (Mo) from outside cellular milieu for maintenance of essential life processes. Mo is serving as cofactor for catalytic activity of xanthine dehydrogenase, aldehyde oxidase and sulphite oxidase from bacteria to mammals. Although Mo transport is well established in prokaryotes and some eukaryotes including plants, little information is available on Mo transport system in mammals. Recently, HsMoT2/MFSD5 was reported to transport Mo by its over expression in HEK-293T cells. But the structural and functional annotation of MoT2/MFSD5 gene product is missing in mammals and still no sequence information is available on farm animals, particularly in buffalo. Here we cloned and sequenced buffalo MoT/MFSD5 and analysed the sequence in silico. We predicted that buffalo MoT is unstable, hydrophobic and trans membrane protein with 50KD molecular weight. It is having 11 trans membrane helices to traverse the cell membrane. Functionally the protein shared sequence homology with a sugar porter family, bovine MFSD5. Three-dimensional model of buffalo MoT was also analysed using Raptor X server that predicted the protein is having two-fold pseudo symmetry between N and C terminal domain. Finally, we performed comparative analysis of buffalo MoT with human and cattle which revealed the protein is highly conserved both structurally and functionally. Thus, the structural and functional annotation of buffalo MoT would pave a way to design suitable mutants or inhibitors which could be exploited to manage Mo deficiency and Mo toxicity in ruminants.