PubMed:10050763 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/10050763","sourcedb":"PubMed","sourceid":"10050763","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/10050763","text":"Synechocystis sp. slr0787 protein is a novel bifunctional enzyme endowed with both nicotinamide mononucleotide adenylyltransferase and 'Nudix' hydrolase activities.\nSynechocystis sp. slr0787 open reading frame encodes a 339 residue polypeptide with a predicted molecular mass of 38.5 kDa. Its deduced amino acid sequence shows extensive homology with known separate sequences of proteins from the thermophilic archaeon Methanococcus jannaschii. The N-terminal domain is highly homologous to the archaeal NMN adenylyltransferase, which catalyzes NAD synthesis from NMN and ATP. The C-terminal domain shares homology with the archaeal ADP-ribose pyrophosphatase, a member of the 'Nudix' hydrolase family. The slr0787 gene has been cloned into a T7-based vector for expression in Escherichia coli cells. The recombinant protein has been purified to homogeneity and demonstrated to possess both NMN adenylyltransferase and ADP-ribose pyrophosphatase activities. Both activities have been characterized and compared to their archaeal counterparts.","tracks":[{"project":"CyanoBase","denotations":[{"id":"T1","span":{"begin":18,"end":25},"obj":"protein"},{"id":"T2","span":{"begin":183,"end":190},"obj":"protein"},{"id":"T3","span":{"begin":707,"end":714},"obj":"protein"}],"attributes":[{"subj":"T1","pred":"source","obj":"CyanoBase"},{"subj":"T2","pred":"source","obj":"CyanoBase"},{"subj":"T3","pred":"source","obj":"CyanoBase"}]}],"config":{"attribute types":[{"pred":"source","value type":"selection","values":[{"id":"CyanoBase","color":"#9393ec","default":true}]}]}}