
Cloning and complete nucleotide sequence of Acinetobacter radioresistens CMC‐1 AglyA gene encoding serine hydroxymethyltransferase
Author(s) -
Hong Ming Chuan,
Wu Mei Li,
Chang Ming Chung
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13402.x
Subject(s) - serine hydroxymethyltransferase , open reading frame , nucleic acid sequence , genetics , gene , biology , homology (biology) , peptide sequence , serine , microbiology and biotechnology , sequence analysis , biochemistry , amino acid , glycine , phosphorylation
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.