中文摘要：

作者在海洋的 Emiliania huxleyi 病毒(EhV-99B1 ) 孤立并且描绘象基因一样的新奇丝氨酸 palmitoyltransferase (SPT ) 。EhV99B1-SPT 的开读物的框架(ORF ) 与 96 kDa 和 Ip 6.01 的一个计算的分子的团编码了 496 氨基酸的蛋白质。顺序分析的结果证明有关于在有另外的有机体的氨基酸顺序的 31%45% 身份的。最大的可能性的种系发生的树建议 EhV99B1-SPT 基因水平地可能从优核质转了。推出的氨基酸序列的恐水病的侧面与五个 transmembrane 领域(TMD ) 建议了恐水病、球状、联系膜的蛋白质主题。几个潜在的连接 N 的 glycosylation 地点在 SPT 被介绍。这些结果建议 EhV99B1-SPT 是不可分的 endoplasmic 蜂窝胃膜蛋白质。尽管有更低的顺序身份，预言的第二等、三维的结构证明袖珍结构元素 2-helices 创作了， 4 表是这酶的催化中心，与在 N 终端区域的一个典型保存 TFTKSFG 活跃地点并且离原核生物的有机体的那些很靠近。然而， EhV99B1-SPT 的 N 终端领域最非常类似于 LCB2 催化作用子单元， C 终端领域最非常类似于 LCB1 哪个的另外的有机体的规章的子单元一起形成了一个球形的分子。这个怪物高度类似于原核生物的相应 SPT。为功能的鉴定， EhV99B1-LCB2 子单元基因在 Escherichia coli 被表示，它在 E 导致了新 sphingolipid 的重要累积。coli 房间。

英文摘要：

The authors have isolated and characterized a novel serine palmitoyltransferase （SPT）-like gene in marine Emiliania huxleyi virus （EhV-99B1）. The open-reading frame （ORF） of EhV99BI-SPT encoded a protein of 496 amino acids with a calculated molecular mass of 96 kDa and Ip 6.01. The results of sequence analysis showed that there was about 31% 45% identity in amino acid sequence with other organisms. The maximum likelihood phylogenetic tree suggested that the EhV99B1-SPT gene possibly horizontally transferred from the eukaryote. Hydrophobic profiles of deduced amino acid sequences suggested a hydrophobic, globular and membrane-associated protein with five transmembrane domains （TMDs） motifs. Several potential N-linked glycosylation sites were presented in SPT. These results suggested that EhV99BI-SPT was an integral endoplasmic reticulum membrane protein. Despite lower sequence identity, the secondary and three-dimensional structures predicted showed that the “pocket” structure element composed of 2a-helices and 4β- sheets was the catalytic center of this enzyme, with a typical conserved “TFTKSFG” active site in the N-terminal region and was very close to those of prokaryotic organisms. However, the N-terminal domain of EhV99B1-SPT most closely resembled the LCB2 catalysis subunit and the C-terminal domain most closely resembled the LCBI regulatory subunit of other organisms which together formed a spherical molecule. This “chimera” was highly similar to the prokaryotic homologous SPT. For a functional identification, the EhV99B1-LCB2 subunit gene was expressed in Escherichia coli, which resulted in significant accumulation of new sphingolipid in E. coli cells.