Protein Domain : Bifunctional pantoate ligase/cytidylate kinase IPR024894

Type	Family
Description	D-Pantothenate is synthesized via four enzymes from ketoisovalerate, which is an intermediate of branched-chain amino acid synthesis [ ]. Pantoate-beta-alanine ligase, also know as pantothenate synthase, (PanC; ) catalyzes the formation of pantothenate from pantoate and alanine in the pantothenate biosynthesis pathway [ ].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 [ , , , , ].Cytidylate kinase ( ) catalyses the phosphorylation of cytidine 5-monophosphate (dCMP) to cytidine 5 -diphosphate (dCDP) in the presence of ATP or GTP. UMP and dCMP can also act as acceptors [ ].This entry represents a bifunctional pantoate ligase/cytidylate kinase resulting from a fusion of the individual enzymes. This fusion has so far only been found in cyanobacteria.
Short Name	Pantoate_ligase/cytidylate_kin