CATH Classification

Domain Context

CATH Clusters

Superfamily Phosphorylase Kinase; domain 1
Functional Family

Enzyme Information

2.7.1.190
Aminoglycoside 2''-phosphotransferase.
based on mapping to UniProt P0A0C1
GTP + gentamicin = GDP + gentamicin 2''-phosphate.
-!- This bacterial enzyme phosphorylates many 4,6-disubstituted aminoglycoside antibiotics that have a hydroxyl group at position 2'', including kanamycin A, kanamycin B, tobramycin, dibekacin, arbekacin, amikacin, gentamicin C, sisomicin and netilmicin. -!- In most, but not all, cases the phosphorylation confers resistance against the antibiotic. -!- Some forms of the enzyme use ATP as a phosphate donor in appreciable amount. -!- The enzyme is often found as a bifunctional enzyme that also catalyzes 6'-aminoglycoside N-acetyltransferase activity. -!- The bifunctional enzyme is the most clinically important aminoglycoside-modifying enzyme in Gram-positive bacteria, responsible for high-level resistance in both Enterococci and Staphylococci.
2.3.1.-
Transferring groups other than amino-acyl groups.
based on mapping to UniProt P0A0C1

UniProtKB Entries (1)

P0A0C1
AACA_STAAU
Staphylococcus aureus
Bifunctional AAC/APH

PDB Structure

PDB 5IQF
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Antibiotic Binding Drives Catalytic Activation of Aminoglycoside Kinase APH(2)-Ia.
Caldwell, S.J., Huang, Y., Berghuis, A.M.
Structure