NUCLEOTIDE-SEQUENCE OF THE RHODOBACTER CAPSULATUS FRUK GENE, WHICH ENCODES FRUCTOSE-1-PHOSPHATE KINASE - EVIDENCE FOR A KINASE SUPERFAMILY INCLUDING BOTH PHOSPHOFRUCTOKINASES OF ESCHERICHIA-COLI
NUCLEOTIDE-SEQUENCE OF THE RHODOBACTER CAPSULATUS FRUK GENE, WHICH ENCODES FRUCTOSE-1-PHOSPHATE KINASE - EVIDENCE FOR A KINASE SUPERFAMILY INCLUDING BOTH PHOSPHOFRUCTOKINASES OF ESCHERICHIA-COLI
复制标题
DOI：
10.1128/jb.173.10.3117-3127.1991
复制
发表时间：
1991-05-01
影响因子：
3.2
通讯作者：
SAIER, MH
中科院分区：
文献类型：
--
作者：
WU, LF;REIZER, A;SAIER, MH
测定了荚膜红细菌果糖（fru）-分解代谢操纵子中编码果糖-1-磷酸激酶（FruK）的fruK基因的序列。Fruk of R.荚膜梭菌（316个氨基酸;分子量= 31，232）与大肠杆菌的FruK、大肠杆菌的磷酸果糖激酶B（Pfk B）大小相同且同源。大肠杆菌的磷酸塔格激酶、金黄色葡萄球菌的磷酸塔格激酶和大肠杆菌的核糖激酶。杆菌因此，这些蛋白质组成了一个同源蛋白质家族，称为PfkB家族。构建了该新家族的系统发育树。序列比较加上化学失活研究表明缺乏参与催化的特定残基。虽然Rhodobacter FruK显着不同的PfkB家族内的其他酶的氨基酸组成，这些酶表现出类似的预测二级结构特征。一个大的内部段的Rhodobacter FruK被发现是相似的序列域轴承的大亚基的核酮糖1，5-二磷酸羧化酶/加氧酶的植物和细菌的糖二磷酸结合区。PfkB家族的蛋白质与大肠杆菌PfkA的蛋白质没有显示统计学上显著的序列同一性。杆菌然而，PfkA与其他原核和真核ATP和PP（i）依赖性Pfks（PfkA家族）同源。这些真核生物的ATP依赖性酶均由同源四聚体（哺乳动物）或异源八聚体（酵母）组成，每个亚基均含有与大肠杆菌PfkA整个蛋白大小相同的内部复制。杆菌在其中一些酶中，存在额外的结构域。构建了PfkA家族的系统发育树，揭示了细菌酶与真核生物酶亚基的N-末端结构域非常相似，而C-末端结构域则更广泛地分化。马铃薯的PP（i）依赖性Pfk与ATP依赖性酶的关系较远。基于它们相似的功能、大小、预测的二级结构和序列，我们认为PfkA和PfkB家族具有共同的进化起源。
The fruK gene encoding fructose-1-phosphate kinase (FruK), located within the fructose (fru)-catabolic operon of Rhodobacter capsulatus, was sequenced. FruK of R. capsulatus (316 amino acids; molecular weight = 31,232) is the same size as and is homologous to FruK of Escherichia coli, phosphofructokinase B (PfkB) of E. coli, phosphotagatokinase of Staphylococcus aureus, and ribokinase of E. coli. These proteins therefore make up a family of homologous proteins, termed the PfkB family. A phylogenetic tree for this new family was constructed. Sequence comparisons plus chemical inactivation studies suggested the lack of involvement of specific residues in catalysis. Although the Rhodobacter FruK differed markedly from the other enzymes within the PfkB family with respect to amino acid composition, these enzymes exhibited similar predicted secondary structural features. A large internal segment of the Rhodobacter FruK was found to be similar in sequence to the domain bearing the sugar bisphosphate-binding region of the large subunit of ribulose 1,5-bisphosphate carboxylase/oxygenase of plants and bacteria. Proteins of the PfkB family did not exhibit statistically significant sequence identity with PfkA of E. coli. PfkA, however, is homologous to other prokaryotic and eukaryotic ATP- and PP(i)-dependent Pfks (the PfkA family). These eukaryotic, ATP-dependent enzymes each consist of a homotetramer (mammalian) or a heterooctamer (yeasts), with each subunit containing an internal duplication of the size of the entire PfkA protein of E. coli. In some of these enzymes, additional domains are present. A phylogenetic tree was constructed for the PfkA family and revealed that the bacterial enzymes closely resemble the N-terminal domains of the eukaryotic enzyme subunits whereas the C-terminal domains have diverged more extensively. The PP(i)-dependent Pfk of potato is only distantly related to the ATP-dependent enzymes. On the basis of their similar functions, sizes, predicted secondary structures, and sequences, we suggest that the PfkA and PfkB families share a common evolutionary origin.