CMPK1
Domain
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Function
Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Also displays broad nucleoside diphosphate kinase activity.
Sequence Similarities
Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.
Tissue Specificity
Ubiquitously expressed.
Cellular localization
- Nucleus
- Cytoplasm
- Predominantly cytoplasmic, less than 15% nuclear.
Alternative names
CMK, CMPK, UCK, UMK, UMPK, CMPK1, UMP-CMP kinase, Deoxycytidylate kinase, Nucleoside-diphosphate kinase, Uridine monophosphate/cytidine monophosphate kinase, CK, dCMP kinase, UMP/CMP kinase, UMP/CMPK