The domain within your query sequence starts at position 1 and ends at position 309; the E-value for the Fructosamin_kin domain shown below is 6e-81.



PFAM accession number:PF03881
Interpro abstract (IPR016477):

Ketosamines derive from a non-enzymatic reaction between a sugar and a protein [ (PUBMED:3319287) ]. Ketosamine-3-kinases (KT3K), of which fructosamine-3-kinase (FN3K) is the best-known example, catalyse the phosphorylation of the ketosamine moiety of glycated proteins. The instability of a phosphorylated ketosamine leads to its degradation, and KT3K is thus thought to be involved in protein repair [ (PUBMED:14633848) ].

The function of the prokaryotic members of this group has not been established. However, several lines of evidence indicate that they may function as fructosamine-3-kinases (FN3K). First, they are similar to characterised FN3K from mouse and human. Second, the Escherichia coli members are found in close proximity on the genome to fructose-6-phosphate kinase (PfkB). Last, FN3K activity has been found in a Anacystis montana (Gloeocapsa montana Kutzing 1843) [ (PUBMED:214181) ], indicating such activity-directly demonstrated in eukaryotes-is nonetheless not confined to eukaryotes.

This family includes eukaryotic fructosamine-3-kinase enzymes [ (PUBMED:11016445) ] which may initiate a process leading to the deglycation of fructoselysine and of glycated proteins and in the phosphorylation of 1-deoxy-1-morpholinofructose, fructoselysine, fructoseglycine, fructose and glycated lysozyme. The family also includes bacterial members that have not been characterised but probably have a similar or identical function.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Fructosamin_kin