AAC6_SALTY
ID AAC6_SALTY Reviewed; 145 AA.
AC Q8ZPB6;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Aminoglycoside N(6')-acetyltransferase type 1 {ECO:0000250|UniProtKB:Q9R381};
DE EC=2.3.1.82 {ECO:0000250|UniProtKB:Q9R381};
DE AltName: Full=AAC(6')-I {ECO:0000250|UniProtKB:Q9R381};
DE AltName: Full=Aminoglycoside resistance protein {ECO:0000250|UniProtKB:Q9R381};
GN OrderedLocusNames=STM1619;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1] {ECO:0000312|EMBL:AAL20537.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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.
CC {ECO:0000250|UniProtKB:Q9R381}.
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:0000250|UniProtKB:Q9R381};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9R381}.
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DR EMBL; AE006468; AAL20537.1; -; Genomic_DNA.
DR RefSeq; NP_460578.1; NC_003197.2.
DR RefSeq; WP_000354865.1; NC_003197.2.
DR AlphaFoldDB; Q8ZPB6; -.
DR SMR; Q8ZPB6; -.
DR STRING; 99287.STM1619; -.
DR PaxDb; Q8ZPB6; -.
DR EnsemblBacteria; AAL20537; AAL20537; STM1619.
DR GeneID; 1253137; -.
DR KEGG; ag:AAL20537; -.
DR KEGG; stm:STM1619; -.
DR PATRIC; fig|99287.12.peg.1710; -.
DR HOGENOM; CLU_127011_0_0_6; -.
DR OMA; DYVNGCS; -.
DR PhylomeDB; Q8ZPB6; -.
DR BioCyc; SENT99287:STM1619-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0047663; F:aminoglycoside 6'-N-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Acyltransferase; Antibiotic resistance; Reference proteome; Transferase.
FT CHAIN 1..145
FT /note="Aminoglycoside N(6')-acetyltransferase type 1"
FT /id="PRO_0000416835"
FT DOMAIN 1..145
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 89..94
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 145 AA; 16376 MW; 4E25311330BCB6BC CRC64;
MDIRQMNRTH LDHWRGLRKQ LWPGHPDDAH LADGEEILQA DHLASFIAMA DGVAIGFADA
SIRHDYVNGC DSSPVVFLEG IFVLPSFRQR GVAKQLIAAV QRWGTNKGCR EMASDTSPEN
TISQKVHQAL GFEETERVIF YRKRC
