ID   AAC6_KLEAE              Reviewed;         152 AA.
AC   P50858;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Aminoglycoside N(6')-acetyltransferase type 1;
DE            EC=2.3.1.82;
DE   AltName: Full=AAC(6')-Il;
DE   AltName: Full=Aminoglycoside resistance protein;
GN   Name=aacA7;
OS   Klebsiella aerogenes (Enterobacter aerogenes).
OG   Plasmid pBWH301.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   PLASMID=pBWH301;
RX   PubMed=7793874; DOI=10.1128/aac.39.3.686;
RA   Bunny K.L., Hall R.M., Stokes H.W.;
RT   "New mobile gene cassettes containing an aminoglycoside resistance gene,
RT   aacA7, and a chloramphenicol resistance gene, catB3, in an integron in
RT   pBWH301.";
RL   Antimicrob. Agents Chemother. 39:686-693(1995).
CC   -!- FUNCTION: Catalyzes the transfer of an acetyl group from acetyl-CoA to
CC       the 6'-amino group of aminoglycoside molecules conferring resistance to
CC       antibiotics containing the purpurosamine ring including amikacin.
CC       {ECO:0000269|PubMed:7793874}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + kanamycin B = CoA + H(+) + N(6')-acetylkanamycin
CC         B; Xref=Rhea:RHEA:16449, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:58390, ChEBI:CHEBI:58549; EC=2.3.1.82;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR   EMBL; U13880; AAA90937.1; -; Genomic_DNA.
DR   RefSeq; WP_013263788.1; NG_047303.1.
DR   AlphaFoldDB; P50858; -.
DR   SMR; P50858; -.
DR   BRENDA; 2.3.1.82; 152.
DR   GO; GO:0047663; F:aminoglycoside 6'-N-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046677; P:response to antibiotic; IDA:UniProtKB.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR024170; Aminoglycoside_N6-AcTrfrase.
DR   InterPro; IPR000182; GNAT_dom.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   PIRSF; PIRSF000452; 6-N-acetyltransf; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Antibiotic resistance; Plasmid; Transferase.
FT   CHAIN           1..152
FT                   /note="Aminoglycoside N(6')-acetyltransferase type 1"
FT                   /id="PRO_0000068555"
FT   DOMAIN          5..152
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   BINDING         26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   152 AA;  16376 MW;  CA2D663D69A867E4 CRC64;
     MDSSPLVRPV ETTDSASWLS MRCELWPDGT CQEHQSEIAE FLSGKVARPA AVLIAVAPDG
     EALGFAELSI RPYAEECYSG NVAFLEGWYV VPSARRQGVG VALVKAAEHW ARGRGCTEFA
     SDTQLTNSAS TSAHLAAGFT EVAQVRCFRK PL