ID   AAC6_ACIBA              Reviewed;         146 AA.
AC   Q43899;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Aminoglycoside N(6')-acetyltransferase type 1 {ECO:0000303|PubMed:7810994};
DE            EC=2.3.1.82 {ECO:0000269|PubMed:7810994};
DE   AltName: Full=AAC(6')-Ih {ECO:0000312|EMBL:AAC41391.1};
DE   AltName: Full=Aminoglycoside resistance protein {ECO:0000250|UniProtKB:P50858};
OS   Acinetobacter baumannii.
OG   Plasmid pIP1858 {ECO:0000269|PubMed:7810994}.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=470;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAC41391.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   SUBSTRATE SPECIFICITY.
RC   STRAIN=BM2686 {ECO:0000312|EMBL:AAC41391.1}; PLASMID=pIP1858;
RX   PubMed=7810994; DOI=10.1128/aac.38.9.1883;
RA   Lambert T., Gerbaud G., Courvalin P.;
RT   "Characterization of the chromosomal aac(6')-Ij gene of Acinetobacter sp.
RT   13 and the aac(6')-Ih plasmid gene of Acinetobacter baumannii.";
RL   Antimicrob. Agents Chemother. 38:1883-1889(1994).
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       kanamycin, tobramycin and netilmicin. {ECO:0000269|PubMed:7810994}.
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:7810994};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9R381}.
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DR   EMBL; L29044; AAC41391.1; -; Genomic_DNA.
DR   PIR; I39503; I39503.
DR   RefSeq; WP_016541245.1; NZ_KP890934.1.
DR   PDB; 4E8O; X-ray; 2.14 A; A/B=1-146.
DR   PDBsum; 4E8O; -.
DR   AlphaFoldDB; Q43899; -.
DR   SMR; Q43899; -.
DR   KEGG; ag:AAC41391; -.
DR   BRENDA; 2.3.1.82; 98.
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   3D-structure; Acyltransferase; Antibiotic resistance; Plasmid; Transferase.
FT   CHAIN           1..146
FT                   /note="Aminoglycoside N(6')-acetyltransferase type 1"
FT                   /id="PRO_0000416833"
FT   DOMAIN          1..146
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   BINDING         22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         81..83
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         120
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   STRAND          2..5
FT                   /evidence="ECO:0007829|PDB:4E8O"
FT   HELIX           11..21
FT                   /evidence="ECO:0007829|PDB:4E8O"
FT   HELIX           26..37
FT                   /evidence="ECO:0007829|PDB:4E8O"
FT   STRAND          42..48
FT                   /evidence="ECO:0007829|PDB:4E8O"
FT   STRAND          54..63
FT                   /evidence="ECO:0007829|PDB:4E8O"
FT   STRAND          72..83
FT                   /evidence="ECO:0007829|PDB:4E8O"
FT   HELIX           85..90
FT                   /evidence="ECO:0007829|PDB:4E8O"
FT   HELIX           92..105
FT                   /evidence="ECO:0007829|PDB:4E8O"
FT   TURN            106..108
FT                   /evidence="ECO:0007829|PDB:4E8O"
FT   STRAND          111..117
FT                   /evidence="ECO:0007829|PDB:4E8O"
FT   HELIX           121..129
FT                   /evidence="ECO:0007829|PDB:4E8O"
FT   STRAND          133..144
FT                   /evidence="ECO:0007829|PDB:4E8O"
SQ   SEQUENCE   146 AA;  16709 MW;  FAA8FBF093B7F1EA CRC64;
     MNIMPISESQ LSDWLALRCL LWPDHEDVHL QEMRQLITQA HRLQLLAYTD TQQAIAMLEA
     SIRYEYVNGT QTSPVAFLEG IFVLPEYRRS GIATGLVQQV EIWAKQFACT EFASDAALDN
     QISHAMHQAL GFHETERVVY FKKNIG