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Information on EC 2.3.1.82 - aminoglycoside 6'-N-acetyltransferase and Organism(s) Staphylococcus warneri and UniProt Accession Q7ATH7

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IUBMB Comments
The antibiotics kanamycin A, kanamycin B, neomycin, gentamicin C1a, gentamicin C2 and sisomicin are substrates. The antibiotic tobramycin, but not paromomycin, can also act as acceptor. The 6-amino group of the purpurosamine ring is acetylated.
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Staphylococcus warneri
UNIPROT: Q7ATH7
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The taxonomic range for the selected organisms is: Staphylococcus warneri
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
aac(6')-ib-cr, aac(6')-ib, aaca-aphd, aac(6'), aac(6')-i, aac(6')-ii, aminoglycoside 6'-n-acetyltransferase, aac(6')-im, aac(6')-ie, aac(6')-ig, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminoglycoside 6'-acetyltransferase-Ie
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AAC(6')
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acetyltransferase, aminoglycoside 6'-N-
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acetyltransferase, kanamycin
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aminoglycoside 6'-N-acetyltransferase
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aminoglycoside-6'-acetyltransferase
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aminoglycoside-6'-N-acetyltransferase
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aminoglycoside-6-N-acetyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:kanamycin-B N6'-acetyltransferase
The antibiotics kanamycin A, kanamycin B, neomycin, gentamicin C1a, gentamicin C2 and sisomicin are substrates. The antibiotic tobramycin, but not paromomycin, can also act as acceptor. The 6-amino group of the purpurosamine ring is acetylated.
CAS REGISTRY NUMBER
COMMENTARY hide
56467-65-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme, with a N-terminal coenzyme A-dependent acetyltransferase domain and a C-terminal GTP-dependent phosphotransferase domain
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AACA_STAWA
479
0
56855
Swiss-Prot
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Acta Crystallogr. Sect. D
70
1561-1571
2014
Staphylococcus warneri (Q7ATH7)
Manually annotated by BRENDA team