ID   AAC6_CITKO              Reviewed;         185 AA.
AC   P10051;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Aminoglycoside N(6')-acetyltransferase type 1;
DE            EC=2.3.1.82;
DE   AltName: Full=AAC(6')-I;
DE   AltName: Full=Aminoglycoside resistance protein;
GN   Name=aacA1;
OS   Citrobacter koseri (Citrobacter diversus).
OG   Plasmid R.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=545;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   PLASMID=R;
RX   PubMed=2826403; DOI=10.1128/jb.170.1.471-473.1988;
RA   Tenover F.C., Filpula D., Phillips K.L., Plorde J.J.;
RT   "Cloning and sequencing of a gene encoding an aminoglycoside 6'-N-
RT   acetyltransferase from an R factor of Citrobacter diversus.";
RL   J. Bacteriol. 170:471-473(1988).
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       kanamycin and tobramycin. {ECO:0000269|PubMed:2826403}.
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; M18967; AAA98298.1; -; Genomic_DNA.
DR   EMBL; M86913; AAA72107.1; -; Genomic_DNA.
DR   PIR; A28677; A28677.
DR   AlphaFoldDB; P10051; -.
DR   SMR; P10051; -.
DR   KEGG; ag:AAA98298; -.
DR   BRENDA; 2.3.1.82; 1399.
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; IPR000182; GNAT_dom.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Antibiotic resistance; Plasmid; Transferase;
KW   Transposable element.
FT   CHAIN           1..185
FT                   /note="Aminoglycoside N(6')-acetyltransferase type 1"
FT                   /id="PRO_0000068552"
FT   DOMAIN          14..183
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   BINDING         34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   185 AA;  21264 MW;  F55FAEF6B301A35B CRC64;
     MNYQIVNIAE CSNYQLEAAN ILTEAFNDLG NNSWPDMTSA TKEVKECIES PNLCFGLLIN
     NSLVGWIGLR PMYKETWELH PLVVRPDYQN KGIGKILLKE LENRAREQGI IGIALGTDDE
     YYRTSLSLIT ITEDNIFDSI KNIKNINKHP YEFYQKNGYY IVGIIPNANG KNKPDIWMWK
     SLIKE