InterPro : IPR023005

Name  Nucleoside diphosphate kinase, active site Short Name  Nucleoside_diP_kinase_AS
Type  Active_site Description  Nucleoside diphosphate kinases () (NDK) are enzymes required for the synthesis of nucleoside triphosphates (NTP) other than ATP. They provide NTPs for nucleic acid synthesis, CTP for lipid synthesis, UTP for polysaccharide synthesis and GTP for protein elongation, signal transduction and microtubule polymerisation. In eukaryotes, there seems to be a small family of NDK isozymes each of which acts in a different subcellular compartment and/or has a distinct biological function. Eukaryotic NDK isozymes are hexamers of two highly related chains (A and B) []. By random association (A6, A5B...AB5, B6), these two kinds of chain form isoenzymes differing in their isoelectric point. NDK are proteins of 17 Kd that act via a ping-pong mechanism in which a histidine residue is phosphorylated, by transfer of the terminal phosphate group from ATP. In the presence of magnesium, the phosphoenzyme can transfer its phosphate group to any NDP, to produce an NTP. NDK isozymes have been sequenced from prokaryotic and eukaryotic sources. It has also been shown []that the Drosophila awd (abnormal wing discs) protein, is a microtubule-associated NDK. Mammalian NDK is also known as metastasis inhibition factor nm23. The sequence of NDK has been highly conserved through evolution. There is a single histidine residue conserved in all known NDK isozymes, which is involved in the catalytic mechanism []. The signature pattern of this entry covers the active site histidine.
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Proteins

InterPro protein domain ID --> Contigs

 

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2 Found In

Id Name Short Name Type
IPR001564 Nucleoside diphosphate kinase Nucleoside_diP_kinase Family
IPR011410 Nucleoside diphosphate kinase, NDK7 NDK7 Family

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2 Publications

First Author Title Year Journal Volume Pages
Biggs J A Drosophila gene that is homologous to a mammalian gene associated with tumor metastasis codes for a nucleoside diphosphate kinase. 1990 Cell 63 933-40
Gilles AM Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. 1991 J Biol Chem 266 8784-9



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)