ID   AAC2_MYCFO              Reviewed;         195 AA.
AC   Q49157;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Aminoglycoside 2'-N-acetyltransferase;
DE            EC=2.3.1.-;
DE   AltName: Full=AAC(2')-Ib;
GN   Name=aac;
OS   Mycolicibacterium fortuitum (Mycobacterium fortuitum).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1766;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FC1K;
RX   PubMed=8891143; DOI=10.1128/aac.40.10.2350;
RA   Ainsa J.A., Martin C., Gicquel B., Gomez-Lus R.;
RT   "Characterization of the chromosomal aminoglycoside 2'-N-acetyltransferase
RT   gene from Mycobacterium fortuitum.";
RL   Antimicrob. Agents Chemother. 40:2350-2355(1996).
CC   -!- FUNCTION: Confers resistance to gentamicin, tobramycin, dibekacin,
CC       netilmicin, and 6'-N-ethylnetilmicin.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the AAC(2')-I acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; U41471; AAC44793.1; -; Genomic_DNA.
DR   RefSeq; WP_003881640.1; NZ_VHPZ01000010.1.
DR   AlphaFoldDB; Q49157; -.
DR   SMR; Q49157; -.
DR   STRING; 1766.XA26_03650; -.
DR   GeneID; 29426913; -.
DR   KEGG; ag:AAC44793; -.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Antibiotic resistance; Transferase.
FT   CHAIN           1..195
FT                   /note="Aminoglycoside 2'-N-acetyltransferase"
FT                   /id="PRO_0000064410"
FT   DOMAIN          21..180
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT   BINDING         92..93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT   BINDING         94..96
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT   BINDING         101..106
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT   BINDING         161..162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQG9"
SQ   SEQUENCE   195 AA;  21343 MW;  A19EC045210D549B CRC64;
     MPFQDVSAPV RGGILHTARL VHTSDLDQET REGARRMVIE AFEGDFSDAD WEHALGGMHA
     FICHHGALIA HAAVVQRRLL YRDTALRCGY VEAVAVREDW RGQGLATAVM DAVEQVLRGA
     YQLGALSASD TARGMYLSRG WLPWQGPTSV LQPAGVTRTP EDDEGLFVLP VGLPAGMELD
     TTAEITCDWR DGDVW