ID   AAC6_SERMA              Reviewed;         201 AA.
AC   P20092;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 74.
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   Serratia marcescens.
OG   Plasmid pAZ007.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-18, FUNCTION, AND
RP   CATALYTIC ACTIVITY.
RC   PLASMID=pAZ007;
RX   PubMed=2824444; DOI=10.1128/jb.169.12.5708-5714.1987;
RA   van Nhieu G.T., Collatz E.;
RT   "Primary structure of an aminoglycoside 6'-N-acetyltransferase AAC(6')-4,
RT   fused in vivo with the signal peptide of the Tn3-encoded beta-lactamase.";
RL   J. Bacteriol. 169:5708-5714(1987).
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 and
CC       kanamycin. {ECO:0000269|PubMed:2824444}.
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:0000269|PubMed:2824444};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR   EMBL; M23634; AAA26550.1; -; Genomic_DNA.
DR   PIR; A28388; A28388.
DR   AlphaFoldDB; P20092; -.
DR   SMR; P20092; -.
DR   BRENDA; 2.3.1.82; 5690.
DR   GO; GO:0047663; F:aminoglycoside 6'-N-acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0046677; P:response to antibiotic; IDA: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   1: Evidence at protein level;
KW   Acyltransferase; Antibiotic resistance; Direct protein sequencing; Plasmid;
KW   Transferase.
FT   CHAIN           1..201
FT                   /note="Aminoglycoside N(6')-acetyltransferase type 1"
FT                   /id="PRO_0000068554"
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;  22579 MW;  EA842ECEE699857C CRC64;
     MSIQHFQRKL GITKYSIVTN SNDSVTLRLM TEHDLAMLYE WLNRSHIVEW WGGEEARPTL
     ADVQEQYLPS VLAQESVTPY IAMLNGEPIG YAQSYVALGS GDGWWEEETD PGVRGIDQLL
     ANASQLGKGL GTKLVRALVE LLFNDPEVTK IQTDPSPSNL RAIRCYEKAG FERQGTVTTP
     DGPAVYMVQT RQAFERTRRF A