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KNTase C-terminal domain
kanamycin nucleotidyltransferase
Identifiers
Symbol	KNTase_C
Pfam	PF07827
Pfam clan	CL0291
InterPro	IPR012481
SCOP2	1kny / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In molecular biology, kanamycin nucleotidyltransferase EC 2.7.7.- (KNTase) is an enzyme which is involved in conferring resistance to aminoglycoside antibiotics. It catalyses the transfer of a nucleoside monophosphate group from a nucleotide to kanamycin. This enzyme is dimeric with each subunit being composed of two domains. The C-terminal domain contains five alpha helices, four of which are organised into an up-and-down alpha helical bundle. Residues found in this domain may contribute to this enzyme's active site.

References

1. Pedersen LC, Benning MM, Holden HM (October 1995). "Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase". Biochemistry. 34 (41): 13305–11. doi:10.1021/bi00041a005. PMID 7577914.

• Protein domains