Literature summary for 2.3.1.82 extracted from

Smith, C.; Toth, M.; Bhattacharya, M.; Frase, H.; Vakulenko, S.
Structure of the phosphotransferase domain of the bifunctional aminoglycoside-resistance enzyme AAC(6)-Ie-APH(2")-Ia (2014), Acta Crystallogr. Sect. D, 70, 1561-1571.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Staphylococcus warneri

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of the N-terminal AAC(6')-Ie enzyme as a ternary kanamycin/coenzyme A abortive complex, to 1,3 A resolution. The AAC(6')-Ie enzyme is joined to the APH(2'')-Ia domain by a short, predominantly rigid linker at the N-terminal end of a long alpha-helix. The presence of the intact alpha-helix is essential to the activity of both functionalities of the full-length AAC(6')-Ie-APH(2'')-Ia enzyme. The two aminoglycoside-binding sites on the bifunctional enzyme are widely separated from each other	Staphylococcus warneri

Crystallization (Comment)

Organism

structure of the N-terminal AAC(6')-Ie enzyme as a ternary kanamycin/coenzyme A abortive complex, to 1,3 A resolution. The AAC(6')-Ie enzyme is joined to the APH(2'')-Ia domain by a short, predominantly rigid linker at the N-terminal end of a long alpha-helix. The presence of the intact alpha-helix is essential to the activity of both functionalities of the full-length AAC(6')-Ie-APH(2'')-Ia enzyme. The two aminoglycoside-binding sites on the bifunctional enzyme are widely separated from each other

Staphylococcus warneri

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus warneri	Q7ATH7	bifunctional enzyme, with a N-terminal coenzyme A-dependent acetyltransferase domain and a C-terminal GTP-dependent phosphotransferase domain	-

Synonyms

Synonyms	Comment	Organism
aacA-aphD	-	Staphylococcus warneri
aminoglycoside 6'-acetyltransferase-Ie	-	Staphylococcus warneri

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Release 2023.1 (January 2023)