Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP. 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1. Homodimer. Forms a trimer of dimers in the crystal. Consists of three domains, an N-terminal domain, a central functional domain, and a unique C-terminal domain containing a zinc knuckle-like motif containing 4 cysteines. Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release. Belongs to the NAPRTase family. Highly divergent. Although this protein is stated to be a nicotinate phosphoribosyltransferase, it has not been functionally characterized, and it might be a quinolinate phosphoribosyltransferase (QPRTase).