InterPro : IPR024894

Name  Bifunctional pantoate ligase/cytidylate kinase Short Name  Pantoate_ligase/cytidylate_kin
Type  Family Description  D-Pantothenate is synthesized via four enzymes from ketoisovalerate, which is anintermediate of branched-chain amino acid synthesis [].Pantoate-beta-alanine ligase, also know as pantothenate synthase, () catalyzes the formation ofpantothenate from pantoate and alanine in the pantothenate biosynthesis pathway [].Cytidylate kinase () catalyzes 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.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

0 Found In

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Briozzo P Structures of escherichia coli CMP kinase alone and in complex with CDP: a new fold of the nucleoside monophosphate binding domain and insights into cytosine nucleotide specificity. 1998 Structure 6 1517-27
Sahm H D-Pantothenate synthesis in Corynebacterium glutamicum and use of panBC and genes encoding L-valine synthesis for D-pantothenate overproduction. 1999 Appl Environ Microbiol 65 1973-9
Sorokin A Sequence analysis of the Bacillus subtilis chromosome region between the serA and kdg loci cloned in a yeast artificial chromosome. 1996 Microbiology 142 ( Pt 8) 2005-16

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)