ID   AAC6_MORMO              Reviewed;         152 AA.
AC   Q15BH7;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Aminoglycoside N(6')-acetyltransferase type 1 {ECO:0000250|UniProtKB:P50858};
DE            EC=2.3.1.82 {ECO:0000250|UniProtKB:P50858};
DE   AltName: Full=AAC(6')-I {ECO:0000250|UniProtKB:P50858};
DE   AltName: Full=Aminoglycoside resistance protein {ECO:0000250|UniProtKB:P50858};
GN   Name=aacA7 {ECO:0000303|PubMed:17341470};
OS   Morganella morganii (Proteus morganii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Morganella.
OX   NCBI_TaxID=582;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ABG23477.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=A209 {ECO:0000269|PubMed:17341470};
RX   PubMed=17341470; DOI=10.1093/jac/dkm020;
RA   Tsakris A., Ikonomidis A., Spanakis N., Poulou A., Pournaras S.;
RT   "Characterization of In3Mor, a new integron carrying VIM-1 metallo-beta-
RT   lactamase and sat1 gene, from Morganella morganii.";
RL   J. Antimicrob. Chemother. 59:739-741(2007).
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 tobramycin and
CC       netilmicin and to a lesser extent to gentamicin and amikacin.
CC       {ECO:0000250|UniProtKB:Q9R381, ECO:0000269|PubMed:17341470}.
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         Evidence={ECO:0000250|UniProtKB:Q9R381};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9R381}.
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DR   EMBL; DQ522239; ABG23477.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q15BH7; -.
DR   SMR; Q15BH7; -.
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; Transferase.
FT   CHAIN           1..152
FT                   /note="Aminoglycoside N(6')-acetyltransferase type 1"
FT                   /id="PRO_0000416831"
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|UniProtKB:Q9R381"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         127
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
SQ   SEQUENCE   152 AA;  16376 MW;  CA2D663D69A867E4 CRC64;
     MDSSPLVRPV ETTDSASWLS MRCELWPDGT CQEHQSEIAE FLSGKVARPA AVLIAVAPDG
     EALGFAELSI RPYAEECYSG NVAFLEGWYV VPSARRQGVG VALVKAAEHW ARGRGCTEFA
     SDTQLTNSAS TSAHLAAGFT EVAQVRCFRK PL