ID   AAC6_STEMA              Reviewed;         153 AA.
AC   Q9RBW7;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Aminoglycoside N(6')-acetyltransferase type 1 {ECO:0000250|UniProtKB:P50858, ECO:0000312|EMBL:AAD52985.1};
DE            EC=2.3.1.82 {ECO:0000269|PubMed:10508008};
DE   AltName: Full=AAC(6')-Iz {ECO:0000312|EMBL:AAD52985.1};
DE   AltName: Full=Aminoglycoside resistance protein {ECO:0000303|PubMed:10508008};
OS   Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas
OS   maltophilia).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=40324;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAD52985.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   SUBSTRATE SPECIFICITY.
RC   STRAIN=BM2690 {ECO:0000269|PubMed:10508008};
RX   PubMed=10508008; DOI=10.1128/aac.43.10.2366;
RA   Lambert T., Ploy M.C., Denis F., Courvalin P.;
RT   "Characterization of the chromosomal aac(6')-Iz gene of Stenotrophomonas
RT   maltophilia.";
RL   Antimicrob. Agents Chemother. 43:2366-2371(1999).
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       gentamicin, kanamycin B, tobramycin, netilmicin, and isepamicin.
CC       {ECO:0000269|PubMed:10508008}.
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:10508008};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9R381}.
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DR   EMBL; AF140221; AAD52985.1; -; Genomic_DNA.
DR   RefSeq; WP_005410660.1; NZ_VLXA01000030.1.
DR   AlphaFoldDB; Q9RBW7; -.
DR   SMR; Q9RBW7; -.
DR   KEGG; ag:AAD52985; -.
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; 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   1: Evidence at protein level;
KW   Acyltransferase; Antibiotic resistance; Transferase.
FT   CHAIN           1..153
FT                   /note="Aminoglycoside N(6')-acetyltransferase type 1"
FT                   /id="PRO_0000416832"
FT   DOMAIN          6..153
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   BINDING         27
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
SQ   SEQUENCE   153 AA;  16516 MW;  2A14BFE0D6DE7A65 CRC64;
     MIASAPTIRQ ATPADAAAWA QLRLGLWPDA DDPLEELTQS LADAEGAVFL ACAADGETVG
     FAEVRLRHDY VNGTESSPVG FLEGWYVQPQ WQGSGVGRAL LAAVQAWTRD AGCRELASDS
     RVEDVQAHAA HRACGFEETE RVVYFRMPLE PSA