Structure and evolution of a multidomain multiphosphoryl transfer protein. Nucleotide sequence of the fruB(HI) gene in Rhodobacter capsulatus and comparisons with homologous genes from other organisms.
Structure and evolution of a multidomain multiphosphoryl transfer protein. Nucleotide sequence of the fruB(HI) gene in Rhodobacter capsulatus and comparisons with homologous genes from other organisms.
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多域多磷酰基转移蛋白的结构和进化。
DOI：
10.1016/s0022-2836(05)80256-6
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发表时间：
1990
影响因子：
5.6
通讯作者：
SaierJr,MH
中科院分区：
文献类型：
--
作者：
Wu,LF;Tomich,JM;SaierJr,MH
The gene order of the fructose (fru) operon and nucleotide sequence of the first gene (fruB(HI)) ofRhodobacter capsulatusare reported, analyzed and compared with homologous genes from other bacteria, and the gene products are identified. Included within the region reported is a gene encoding a multiphosphoryl transfer protein (MTP) of the phosphoenolpyruvate: sugar phosphotransferase system (PTS). MTP consists of three moieties: a fructose-specific enzyme III (IIIfru)-like N-terminal moiety (residues 1 to 143) followed by an FPr(HPr)-like moiety (residues 157 to 245) and an enzyme I-like moiety (residues 273 to 827). The enzyme III-like moiety closely resembles the N-terminal 143 residues of the IIIfru-FPR fusion protein fromSalmonella typhimurium(40·6% identity throughout its length) and the C-terminal 145 residues of the mannitol-specific enzyme II (IImtl) (37·8% identity throughout its length with the IIImtlmoiety of IImtl). The FPr-like domain of MTP resembles theS. typhimuriumFPr (42·4% identity) and theEscherichia coliorS. typhimuriumHPr (38·8% identity). The enzyme I-like moiety resembles theE. colienzyme I (38·9% identity). Predicted phosphorylation sites within the three functional units of MTP (His62 in the IIIfru-like moiety; Hiauthor71 in the FPr-like moiety and HiThe gene order of the fructose (fru) operon and nucleotide sequence of the first gene (fruB(HI)) ofRhodobacter capsulatusare reported, analyzed and compared with homologous genes from other bacteria, and the gene products are identified. Included within the region reported is a gene encoding a multiphosphoryl transfer protein (MTP) of the phosphoenolpyruvate: sugar phosphotransferase system (PTS). MTP consists of three moieties: a fructose-specific enzyme III (IIIfru)-like N-terminal moiety (residues 1 to 143) followed by an FPr(HPr)-like moiety (residues 157 to 245) and an enzyme I-like moiety (residues 273 to 827). The enzyme III-like moiety closely resembles the N-terminal 143 residues of the IIIfru-FPR fusion protein fromSalmonella typhimurium(40·6% identity throughout its length) and the C-terminal 145 residues of the mannitol-specific enzyme II (IImtl) (37·8% identity throughout its length with the IIImtlmoiety of IImtl). The FPr-like domain of MTP resembles theS. typhimuriumFPr (42·4% identity) and theEscherichia coliorS. typhimuriumHPr (38·8% identity). The enzyme I-like moiety resembles theE. colienzyme I (38·9% identity). Predicted phosphorylation sites within the three functional units of MTP (His62 in the IIIfru-like moiety; Hiauthor71 in the FPr-like moiety and HiThe gene order of the fructose (fru) operon and nucleotide sequence of the first gene (fruB(HI)) ofRhodobacter capsulatusare reported, analyzed and compared with homologous genes from other bacteria, and the gene products are identified. Included within the region reported is a gene encoding a multiphosphoryl transfer protein (MTP) of the phosphoenolpyruvate: sugar phosphotransferase system (PTS). MTP consists of three moieties: a fructose-specific enzyme III (IIIfru)-like N-terminal moiety (residues 1 to 143) followed by an FPr(HPr)-like moiety (residues 157 to 245) and an enzyme I-like moiety (residues 273 to 827). The enzyme III-like moiety closely resembles the N-terminal 143 residues of the IIIfru-FPR fusion protein fromSalmonella typhimurium(40·6% identity throughout its length) and the C-terminal 145 residues of the mannitol-specific enzyme II (IImtl) (37·8% identity throughout its length with the IIImtlmoiety of IImtl). The FPr-like domain of MTP resembles theS. typhimuriumFPr (42·4% identity) and theEscherichia coliorS. typhimuriumHPr (38·8% identity). The enzyme I-like …
