Xu Yuquan, Chen Ming, Zhang Wei, Lin Min
Department of Biotechnology, Institute for Application of Atomic Energy, Chinese Academy of Agricultural Sciences, P. O. Box 5109, Beijing, 100094, China.
Curr Microbiol. 2003 Apr;46(4):235-40. doi: 10.1007/s00284-002-3840-4.
Acinetobacter calcoaceticus PHEA-2 is a phenol-degrading bacterium isolated from the wastewater from an oil refinery. A 10-kb XhoI fragment consisting of nine complete Open Reading Frames (ORFs) and one partial ORF was screened from a lambda library of PHEA-2 by Southern hybridization. The sequence analyses revealed that ORF2-ORF7, designated mphKLMNOP, are homologous to dmpKLMNOP of Pseudomonas sp. CF600 and mopKLMNOP of Acinetobacter calcoaceticus NCIB8250, sharing 38%-72% and 58.5%-93.5% respectively. The products encoded by dmp and mop genes convert phenol to catechol. The mph-operon and downstream ORFs, ORF9 and ORF10, sharing high identities to benM and benA, which encode ben-operon regulatory protein and benzoate 1,2-dioxygenase alpha subunit respectively, are separated by ORF8, whose function is unknown. The organization of the mph and ben operons is different from that described previously.
醋酸钙不动杆菌PHEA-2是从炼油厂废水中分离出的一种苯酚降解菌。通过Southern杂交从PHEA-2的λ文库中筛选出一个由9个完整开放阅读框(ORF)和1个部分ORF组成的10 kb XhoI片段。序列分析表明,命名为mphKLMNOP的ORF2-ORF7与假单胞菌属CF600的dmpKLMNOP和醋酸钙不动杆菌NCIB8250的mopKLMNOP同源,相似度分别为38%-72%和58.5%-93.5%。dmp和mop基因编码的产物将苯酚转化为邻苯二酚。mph操纵子及下游的ORF9和ORF10与benM和benA具有高度同源性,分别编码ben操纵子调节蛋白和苯甲酸1,2-双加氧酶α亚基,它们被功能未知的ORF8隔开。mph和ben操纵子的结构与先前描述的不同。