Untitled

Abstract

Tannase (Tannin acyl hydrolase, EC 3.1.1.20), an industrially important enzyme, is predominantly produced by bacteria as well as fungi. Present study reports evolutionary relatedness among 112 fungal tannase protein sequences through superfamily/family search and protein sequences based phylogenetic analysis. Although all the selected tannase sequences belonged to alpha/beta-Hydrolase superfamily, but they were distributed in different families. Most of the Auricularia were related to Haloperoxidase family but maximum Aspergillus sp. showed relation with Hypothetical protein TT16620 family. This differentiation was also observed in phylogenetic analysis where Auricularia sp. and Stereum sp.were found in one cluster and Aspergillus sp. in another cluster thus indicating prominent sequence divergency.Comparison among whole protein and domain based phylogeny revealed gradual separation of related species in different blocks followed by species specific functional tannase motif identification. A total of 85 sequences were found with six common blocks among which block 2 and 4 showed relation with tannase function. Again motif 1 of block 2 (KTYWNGCSTGGREGMKQVQRF) and motif 1 of block 4 (FQERGGKMIHYHGEAD PCIPTANSVHYWQ) also showed tannase function, which could be used for species specific probe designing on PCR amplification. Subcellular localization of fungal tannase protein sequences revealed that most of the sequences were secretory in nature. Localization study will disclose the metabolic network of fungal tannase associated with mitochondria and other organelle too. Sequence and structure based analysis of Auricularia delicata (Acc. No. EJD47898.1) and Aspergillus kawachii (Acc. No. GAA89804.1) tannase protein indicated structures are more conserved than sequences and the diversity occurs at loop positions.Banerjee et al RJLBPCS 2017