AAC6_SALEN
ID AAC6_SALEN Reviewed; 145 AA.
AC Q9R381;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Aminoglycoside N(6')-acetyltransferase type 1 {ECO:0000250|UniProtKB:P50858};
DE EC=2.3.1.82 {ECO:0000269|PubMed:10542165, ECO:0000269|PubMed:15123251};
DE AltName: Full=AAC(6')-Iy {ECO:0000250|UniProtKB:P50858};
DE AltName: Full=Aminoglycoside resistance protein {ECO:0000250|UniProtKB:P50858};
OS Salmonella enteritidis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=149539;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF03532.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=BM4361 {ECO:0000312|EMBL:AAF03531.1}, and
RC BM4362 {ECO:0000312|EMBL:AAF03532.1};
RX PubMed=10542165; DOI=10.1128/jb.181.21.6650-6655.1999;
RA Magnet S., Courvalin P., Lambert T.;
RT "Activation of the cryptic aac(6')-Iy aminoglycoside resistance gene of
RT Salmonella by a chromosomal deletion generating a transcriptional fusion.";
RL J. Bacteriol. 181:6650-6655(1999).
RN [2] {ECO:0000305, ECO:0000312|PDB:1S5K}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEXES WITH COENZYME A AND
RP SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, SUBUNIT, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15123251; DOI=10.1016/j.chembiol.2004.03.017;
RA Vetting M.W., Magnet S., Nieves E., Roderick S.L., Blanchard J.S.;
RT "A bacterial acetyltransferase capable of regioselective N-acetylation of
RT antibiotics and histones.";
RL Chem. Biol. 11:565-573(2004).
RN [3] {ECO:0000305, ECO:0000312|PDB:2VBQ}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR, AND
RP CATALYTIC ACTIVITY.
RX PubMed=18095712; DOI=10.1021/bi701957c;
RA Magalhaes M.L., Vetting M.W., Gao F., Freiburger L., Auclair K.,
RA Blanchard J.S.;
RT "Kinetic and structural analysis of bisubstrate inhibition of the
RT Salmonella enterica aminoglycoside 6'-N-acetyltransferase.";
RL Biochemistry 47:579-584(2008).
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 tobramycin, dibekacin and ribostamycin. Able to acetylate eukaryotic
CC histone proteins. {ECO:0000269|PubMed:10542165,
CC ECO:0000269|PubMed:15123251}.
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:10542165, ECO:0000269|PubMed:15123251,
CC ECO:0000269|PubMed:18095712};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15123251,
CC ECO:0000269|PubMed:18095712}.
CC -!- CAUTION: Strain BM4361 does not express or weakly expresses
CC aminoglycoside resistance gene and is thus aminoglycoside-sensitive.
CC Strain BM4362 expresses it due to a chromosomal deletion leading to
CC aminoglycoside resistance. {ECO:0000269|PubMed:10542165}.
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DR EMBL; AF144880; AAF03531.1; -; Genomic_DNA.
DR EMBL; AF144881; AAF03532.1; -; Genomic_DNA.
DR RefSeq; WP_000354853.1; NZ_JYXI01000003.1.
DR PDB; 1S3Z; X-ray; 2.00 A; A/B=1-145.
DR PDB; 1S5K; X-ray; 2.40 A; A/B=1-145.
DR PDB; 1S60; X-ray; 3.00 A; A=1-145.
DR PDB; 2VBQ; X-ray; 2.00 A; A/B=1-145.
DR PDBsum; 1S3Z; -.
DR PDBsum; 1S5K; -.
DR PDBsum; 1S60; -.
DR PDBsum; 2VBQ; -.
DR AlphaFoldDB; Q9R381; -.
DR SMR; Q9R381; -.
DR DrugBank; DB01992; Coenzyme A.
DR DrugBank; DB03615; Ribostamycin.
DR KEGG; ag:AAF03531; -.
DR PATRIC; fig|149539.391.peg.3256; -.
DR EvolutionaryTrace; Q9R381; -.
DR GO; GO:0047663; F:aminoglycoside 6'-N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IDA:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; 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; Transferase.
FT CHAIN 1..145
FT /note="Aminoglycoside N(6')-acetyltransferase type 1"
FT /id="PRO_0000416829"
FT DOMAIN 1..145
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15123251"
FT BINDING 25
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15123251,
FT ECO:0000269|PubMed:18095712"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15123251,
FT ECO:0000269|PubMed:18095712"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15123251,
FT ECO:0000269|PubMed:18095712"
FT BINDING 81..83
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:15123251,
FT ECO:0000269|PubMed:18095712"
FT BINDING 89..94
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:15123251,
FT ECO:0000269|PubMed:18095712"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15123251,
FT ECO:0000269|PubMed:18095712"
FT BINDING 120
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:15123251,
FT ECO:0000269|PubMed:18095712"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15123251,
FT ECO:0000269|PubMed:18095712"
FT STRAND 1..5
FT /evidence="ECO:0007829|PDB:1S3Z"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:1S3Z"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:1S3Z"
FT HELIX 27..39
FT /evidence="ECO:0007829|PDB:1S3Z"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:1S3Z"
FT STRAND 53..63
FT /evidence="ECO:0007829|PDB:1S3Z"
FT STRAND 71..83
FT /evidence="ECO:0007829|PDB:1S3Z"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1S3Z"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1S3Z"
FT HELIX 92..106
FT /evidence="ECO:0007829|PDB:1S3Z"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:1S3Z"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:1S3Z"
FT STRAND 133..144
FT /evidence="ECO:0007829|PDB:1S3Z"
SQ SEQUENCE 145 AA; 16362 MW; 9CD8BBFD48BC43A2 CRC64;
MDIRQMNKTH LEHWRGLRKQ LWPGHPDDAH LADGEEILQA DHLASFIAMA DGVAIGFADA
SIRHDYVNGC DSSPVVFLEG IFVLPSFRQR GVAKQLIAAV QRWGTNKGCR EMASDTSPEN
TISQKVHQAL GFEETERVIF YRKRC
