Structural heterogeneity assessment among the isoforms of fungal 1-aminocyclopropane-1-carboxylic acid (ACC) deaminase: a comparative in silico perspective

Abstract

Abstract Background The primary amino acid sequence of a protein is a translated version from its gene sequence which carries important messages and information concealed therein. The present study unveils the structure-function and evolutionary aspects of 1-aminocyclopropane-1-carboxylic acid deaminase (ACCD) proteins of fungal origin. ACCD, an important plant growth-promoting microbial enzyme, is less frequent in fungi compared to bacteria. Hence, an inclusive understanding of fungal ACC deaminases (fACCD) has brought forth here. Results In silico investigation of 40 fACCD proteins recovered from NCBI database reveals that fACCD are prevalent in Colletotrichum (25%), Fusarium (15%), and Trichoderma (10%). The fACCD were found 16.18–82.47 kDa proteins having 149–750 amino acid residues. The enzyme activity would be optimum in a wide range of pH having isoelectric points 4.76–10.06. Higher aliphatic indices (81.49–100.13) and instability indices > 40 indicated the thermostability nature. The secondary structural analysis further validates the stability owing to higher α-helices. Built tertiary protein models designated as ACCNK1–ACCNK40 have been deposited in the PMDB with accessions PM0083418–39 and PM0083476–93. All proteins were found as homo-dimer except ACCNK13, a homo-tetramer. Conclusions Hence, these anticipated features would facilitate to explore and identify novel variants of fungal ACCD in vitro aiming to industrial-scale applications.