Aminoglycoside 3-phosphotransferase (IPR024165)

Short name: Kan/Strep_kinase

Overlapping homologous superfamilies

Family relationships



Aminoglycoside antibiotics constitute an important class of clinically useful drugs, including gentamicin, tobramycin, and streptomycin, which are used in the treatment of a variety of bacterial infections [PMID: 9872733]. They work by targeting the bacterial ribosome and causing mistranslation of mRNA, leading to the production of defective proteins. In many cases these defective proteins insert into the cell membrane, causing a loss of membrane integrity and precipitating cell death. The most common cause of resistance to these antibiotics is their modification by acetylating, adenylating or phosphorylating enzymes.

This entry represents aminoglycoside 3'-phosphotransferases, one of the best characterised aminoglycoside-resistance enzyme families. These enzymes transfer a phophoryl group from ATP to the 3' position of the aminoglycoside molecule. Studies indicate that these enzymes are both structurally and functionally homologous to eukaryotic protein kinases [PMID: 11467935, PMID: 12006485, PMID: 12628253]. The enzyme contains two domains, an N-terminal domain composed mainly of an antiparallel beta sheet, and a C-terminal domain which is largely alpha helical. The active site lies between these domains and comprises both the ATP binding site and the aminoglycoside binding site.

GO terms

Biological Process

GO:0046677 response to antibiotic

Molecular Function

GO:0005524 ATP binding
GO:0016773 phosphotransferase activity, alcohol group as acceptor

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.