title: The complete nucleotide sequence of the Escherichia coli gene appA reveals significant homology between pH 2.5 acid phosphatase and glucose-1-phosphatase.
abstract: The whole nucleotide sequence of Escherichia coli gene appA, which encodes periplasmic phosphoanhydride phosphohydrolase (optimum pH, 2.5), and its flanking regions was determined. The AppA protein is significantly homologous to the product of the nearby gene agp, acid glucose-1-phosphatase. Because identical amino acids are distributed over the whole lengths of the proteins, it is likely that appA and agp originate from the same ancestor gene.
authors.affiliation: Service de Biochimie, Département de Biologie, Gif-sur-Yvette, France.
authors.forename: J
authors.initials: J
authors.lastname: Dassa
authors.forename: C
authors.initials: C
authors.lastname: Marck
authors.forename: P L
authors.initials: PL
authors.lastname: Boquet
mesh_terms: D000135:Acid Phosphatase / Q000235:genetics*; D000595:Amino Acid Sequence; D001483:Base Sequence; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D010744:Phosphoric Monoester Hydrolases / Q000235:genetics*; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid
chemical_list: D029968:Escherichia coli Proteins; C062887:agp protein, E coli; D000135:Acid Phosphatase; D010744:Phosphoric Monoester Hydrolases