1st International and 10th National Iranian Conference on Bioinformatics
Home Accepted Papers
In silico analysis of the deduced protein sequence of eugenol o-methyltransferase of Ocimum basilicum L.
Paper ID : 1321-ICB10
Authors:
Fatemeh Khakdan *1, Mohammad Rafiei2
1گروه زیست شناسی، پردیس فرزانگان، دانشگاه سمنان، سمنان
2گروه بیوتکنولوژی، دانشگاه صنعتی اصفهان
Abstract:
Eugenol are the principal bioactive components of the defensive arsenal of the Ocimum species, which act as signal molecules among plants, humans, and microbes [1]. The final stage in the biosynthesis of phenylpropene, methyl eugenol is catalysis by eugenol O-methyltransferase (EOMT) enzyme [2]. The phylogenetic results indicated different EOMT form evolving from a single ancestral gene and resulting tree was classified into four clusters. ObEOMT was found associated with O. tenuiflorum. The ObEOMT protein molecular mass was predicted to be about 40236.52 and the isoelectric point was predicted to be at 5.59 calculated by the Online Computer pI/MW Tool (http://cn.expasy.org/tools). In addition, based on InterProScan tool and pfam database, the putative amino acids sequence revealed more homology with conserved active site consensus sequence at the N terminus of a variety of plant O-methyltransferases (MSLKCAIQLGIPDILHKHGRPMTLSQLLQSIPINKEKTQCFQRLMRALV) to mediate dimerisation and methyltransferase of these proteins. As PROSITE motif search show, ObEOMT have four major motifs, ASN_GLYCOSYLATION (consisting of 116 amino acids; N-{P}-[ST]-{P}), PKC_PHOSPHO_SITE (Protein kinase C phosphorylation site; [ST]-x-[RK]), CK2_PHOSPHO_SITE (Casein kinase II phosphorylation site; [ST]-x(2)-[DE]), and MYRISTYL (N-myristoylation site; Ala, Ser, Thr, Cys, Asn and Gly). According to conserved domain database, the ProDom and TrEMBL results showed ObEOMT protein consist of the essential domain, EQLLQAQVHVWNHMYAFANSMSLKCAIQLGIPDILHKHGRPMTLS has been specified in SAM-dependent O-methyltransferase class II-type profile. PSORT, signal P and Target P analyses showed the presence of a GxG motif in the N-terminal region of ObEOMT amino acid sequence, which was not found in the protein localization signal peptide at the C-terminal region. Results revealed that predicted ObEOMT protein was a predominantly α-helical protein, which mainly consisted of alpha helices (49.3%) and random coils (27.22%), extended strands (12.9%), and 37.8% beta turns [3].
Keywords:
eugenol O-methyltransferase (EOMT); phylogenetic analysis; conserved domains; catalytic domains; motif prediction
Status : Paper Accepted (Poster Presentation)