AAC6C_SERMA
ID AAC6C_SERMA Reviewed; 146 AA.
AC Q54441;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Aminoglycoside N(6')-acetyltransferase type 1 {ECO:0000303|PubMed:1354954, ECO:0000312|EMBL:AAA26549.1};
DE EC=2.3.1.82 {ECO:0000269|PubMed:1354954};
DE AltName: Full=AAC(6')-Ic {ECO:0000312|EMBL:AAA26549.1};
DE AltName: Full=Aminoglycoside resistance protein {ECO:0000250|UniProtKB:P50858};
OS Serratia marcescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAA26549.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=SM16 {ECO:0000269|PubMed:1354954};
RX PubMed=1354954; DOI=10.1128/aac.36.7.1447;
RA Shaw K.J., Rather P.N., Sabatelli F.J., Mann P., Munayyer H., Mierzwa R.,
RA Petrikkos G.L., Hare R.S., Miller G.H., Bennett P.;
RT "Characterization of the chromosomal aac(6')-Ic gene from Serratia
RT marcescens.";
RL Antimicrob. Agents Chemother. 36:1447-1455(1992).
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, netilmicin, isepamicin and sisomicin.
CC {ECO:0000269|PubMed:1354954}.
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:1354954};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9R381}.
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DR EMBL; M94066; AAA26549.1; -; Genomic_DNA.
DR PIR; A48897; A48897.
DR RefSeq; WP_033649026.1; NZ_VKXL01000008.1.
DR AlphaFoldDB; Q54441; -.
DR SMR; Q54441; -.
DR STRING; 273526.SMDB11_3538; -.
DR KEGG; ag:AAA26549; -.
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_0000416834"
FT DOMAIN 1..146
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 21
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 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; 16281 MW; A9555B616ED021C3 CRC64;
MIVICDHDNL DAWLALRTAL WPSGSPEDHR AEMREILASP HHTAFMARGL DGAFVAFAEV
ALRYDYVNGC ESSPVAFLEG IYTAERARRQ GWAARLIAQV QEWAKQQGCS ELASDTDIAN
LDSQRLHAAL GFAETERVVF YRKTLG
