AAC6_ACIG1
ID AAC6_ACIG1 Reviewed; 146 AA.
AC Q44245;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 68.
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')-Ij {ECO:0000312|EMBL:AAC41392.1};
DE AltName: Full=Aminoglycoside resistance protein {ECO:0000250|UniProtKB:P50858};
OS Acinetobacter genomosp. 13.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=72607;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC41392.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=BM2689 {ECO:0000312|EMBL:AAC41392.1};
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}.
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DR EMBL; L29045; AAC41392.1; -; Genomic_DNA.
DR RefSeq; WP_016651650.1; NG_047301.1.
DR AlphaFoldDB; Q44245; -.
DR SMR; Q44245; -.
DR GeneID; 45418978; -.
DR KEGG; ag:AAC41392; -.
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..146
FT /note="Aminoglycoside N(6')-acetyltransferase type 1"
FT /id="PRO_0000416836"
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"
SQ SEQUENCE 146 AA; 16688 MW; 12DE9D036F87BDFF CRC64;
MNIMPVSESL MADWLGLRKL LWPDHDEAHL QEMQRLLQQT QSLQLLAYSD TQQAIAMLEA
SIRYEYVNGT QTSPVAFLEG IYVLPDYRRS GIATHLVQQV EAWAKPFGCI EFASDAALDN
RISHAMHQAL GFHETERVVY FKKHIG
