InterPro domain: IPR003721

D-Pantothenate is synthesized via four enzymes from ketoisovalerate, which is an intermediate of branched-chain amino acid synthesis [ 1 ]. Pantoate-beta-alanine ligase, also know as pantothenate synthase, (PanC; 6.3.2.1 ) catalyzes the formation of pantothenate from pantoate and alanine in the pantothenate biosynthesis pathway [ 2 ].

PanC belongs to a large superfamily of nucleotidyltransferases that includes ATP sulfurylase (ATPS), phosphopantetheine adenylyltransferase (PPAT), and the amino-acyl tRNA synthetases. The enzymes of this family are structurally similar and share a dinucleotide-binding domain [ 3 , 4 , 5 , 6 , 7 ].

1. D-Pantothenate synthesis in Corynebacterium glutamicum and use of panBC and genes encoding L-valine synthesis for D-pantothenate overproduction. Appl. Environ. Microbiol. 65, 1973-9
2. Sequence analysis of the Bacillus subtilis chromosome region between the serA and kdg loci cloned in a yeast artificial chromosome. Microbiology (Reading, Engl.) 142 ( Pt 8), 2005-16
3. Biosynthesis of pantothenate. Nat Prod Rep 21, 695-721
4. The cytidylyltransferase superfamily: identification of the nucleotide-binding site and fold prediction. Proteins 22, 259-66
5. Pantothenate synthetase from Escherichia coli [D-pantoate: beta-alanine ligase (AMP-forming), EC 6.3.2.1]. Meth. Enzymol. 62, 215-9
6. Genetic and biochemical analyses of pantothenate biosynthesis in Escherichia coli and Salmonella typhimurium. J. Bacteriol. 149, 916-22
7. The final step of pantothenate biosynthesis in higher plants: cloning and characterization of pantothenate synthetase from Lotus japonicus and Oryza sativum (rice). Biochem. J. 341 ( Pt 3), 669-78