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AAC6_KLEPN
ID   AAC6_KLEPN              Reviewed;         201 AA.
AC   P19650;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=aacA4;
OS   Klebsiella pneumoniae.
OG   Plasmid pJHC-MW1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   TRANSPOSON=Tn1331;
RX   PubMed=2841303; DOI=10.1128/jb.170.8.3769-3773.1988;
RA   Nobuta K., Tolmasky M.E., Crosa L.M., Crosa J.H.;
RT   "Sequencing and expression of the 6'-N-acetyltransferase gene of transposon
RT   Tn1331 from Klebsiella pneumoniae.";
RL   J. Bacteriol. 170:3769-3773(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TRANSPOSON=Tn1331;
RX   PubMed=1963948; DOI=10.1016/0147-619x(90)90005-w;
RA   Tolmasky M.E.;
RT   "Sequencing and expression of aadA, bla, and tnpR from the multiresistance
RT   transposon Tn1331.";
RL   Plasmid 24:218-226(1990).
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:2841303}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA69748.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; M21682; AAA69747.1; -; Genomic_DNA.
DR   EMBL; M21682; AAA69748.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M55547; AAA98404.1; -; Genomic_DNA.
DR   PIR; B31104; B31104.
DR   RefSeq; NP_608307.1; NC_003486.1.
DR   RefSeq; WP_004152783.1; NZ_WMJK01000045.1.
DR   RefSeq; YP_001928078.1; NC_010726.1.
DR   RefSeq; YP_001928081.1; NC_010726.1.
DR   RefSeq; YP_002286819.1; NC_011382.1.
DR   RefSeq; YP_006958960.1; NC_019156.1.
DR   RefSeq; YP_006959190.1; NC_019159.1.
DR   RefSeq; YP_008146463.1; NC_021656.1.
DR   RefSeq; YP_008166967.1; NC_021666.1.
DR   AlphaFoldDB; P19650; -.
DR   SMR; P19650; -.
DR   KEGG; ag:AAA69747; -.
DR   BRENDA; 2.3.1.82; 2814.
DR   GO; GO:0047663; F:aminoglycoside 6'-N-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046677; P:response to antibiotic; IMP:UniProtKB.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR030971; N6_acetyl_AAC6.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR04431; N6_acetyl_AAC6; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Antibiotic resistance; Plasmid; Transferase;
KW   Transposable element.
FT   CHAIN           1..201
FT                   /note="Aminoglycoside N(6')-acetyltransferase type 1"
FT                   /id="PRO_0000068553"
FT   DOMAIN          25..192
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   BINDING         51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   201 AA;  22407 MW;  ED0314DCDF05BEDC CRC64;
     MSIQHFQTKL GITKYSIVTN SNDSVTLRLM TEHDLAMLYE WLNRSHIVEW WGGEEARPTL
     ADVQEQYLPS VLAQESVTPY IAMLNGEPIG YAQSYVALGS GDGWWEEETD PGVRGIDQLL
     ANASQLGKGL GTKLVRALVE LLFNDPEVTK IQTDPSPSNL RAIRCYEKAG FERQGTVTTP
     DGPAVYMVQT RQAFERTRSV A
 
 
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