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