Hong M C, Wu M L, Chang M C
Department of Biochemistry, Medical College, National Cheng Kung University, Tainan, Taiwan.
FEMS Microbiol Lett. 1999 Jan 15;170(2):413-8. doi: 10.1111/j.1574-6968.1999.tb13402.x.
A gene (AglyA) encoding serine hydroxymethyltransferase of Acinetobacter radioresistens CMC-1 was cloned and sequenced. Nucleotide sequence analysis of AglyA predicted a single open reading frame (ORF) of 1251 bp encoding a 417-amino acid polypeptide. Two putative MetR-like binding sites (5'-TGAAACATGAGCT) and (5'-TGAGCAAAGTTCA), centered at bp -123 and -95 relative to the +1 translation start site were found, which have six out of nine and eight out of nine nucleotides that match to the consensus sequence of Escherichia coli (5'-TGAANNT/ANNTTCA), respectively. The enzyme also showed a high level of homology to other sources of serine hydroxymethyltransferase proteins.
对耐辐射不动杆菌CMC-1编码丝氨酸羟甲基转移酶的基因(AglyA)进行了克隆和测序。AglyA的核苷酸序列分析预测有一个1251 bp的单一开放阅读框(ORF),编码一个417个氨基酸的多肽。发现了两个假定的类MetR结合位点(5'-TGAAACATGAGCT)和(5'-TGAGCAAAGTTCA),相对于+1翻译起始位点,其中心分别位于-123和-95 bp处,分别有9个核苷酸中的6个和9个核苷酸中的8个与大肠杆菌的共有序列(5'-TGAANNT/ANNTTCA)匹配。该酶与其他来源的丝氨酸羟甲基转移酶蛋白也显示出高度同源性。