AAC2_MYCS2
ID AAC2_MYCS2 Reviewed; 210 AA.
AC P94968; A0QPK9; I7G383;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Aminoglycoside 2'-N-acetyltransferase;
DE EC=2.3.1.- {ECO:0000269|PubMed:9159528};
DE AltName: Full=AAC(2')-Id;
GN Name=aac; OrderedLocusNames=MSMEG_0434, MSMEI_0423;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9159528; DOI=10.1046/j.1365-2958.1997.3471717.x;
RA Ainsa J.A., Perez E., Pelicic V., Berthet F.-X., Gicquel B., Martin C.;
RT "Aminoglycoside 2'-N-acetyltransferase genes are universally present in
RT mycobacteria: characterization of the aac(2')-Ic gene from Mycobacterium
RT tuberculosis and the aac(2')-Id gene from Mycobacterium smegmatis.";
RL Mol. Microbiol. 24:431-441(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
CC -!- FUNCTION: Catalyzes the coenzyme A-dependent acetylation of the 2'
CC hydroxyl or amino group of a broad spectrum of aminoglycosides. It
CC confers resistance to aminoglycosides. {ECO:0000269|PubMed:9159528}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AAC(2')-I acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U72743; AAB41701.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK70574.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP36904.1; -; Genomic_DNA.
DR RefSeq; WP_011726942.1; NZ_SIJM01000025.1.
DR RefSeq; YP_884847.1; NC_008596.1.
DR PDB; 7CRM; X-ray; 2.49 A; A/B/C/D=1-210.
DR PDB; 7CS0; X-ray; 2.05 A; A/B=1-210.
DR PDB; 7CS1; X-ray; 1.97 A; A/B=1-210.
DR PDB; 7CSI; X-ray; 1.89 A; A/B=1-210.
DR PDB; 7CSJ; X-ray; 2.17 A; A/B=1-210.
DR PDBsum; 7CRM; -.
DR PDBsum; 7CS0; -.
DR PDBsum; 7CS1; -.
DR PDBsum; 7CSI; -.
DR PDBsum; 7CSJ; -.
DR AlphaFoldDB; P94968; -.
DR SMR; P94968; -.
DR STRING; 246196.MSMEI_0423; -.
DR EnsemblBacteria; ABK70574; ABK70574; MSMEG_0434.
DR EnsemblBacteria; AFP36904; AFP36904; MSMEI_0423.
DR GeneID; 66738619; -.
DR KEGG; ag:AAB41701; -.
DR KEGG; msg:MSMEI_0423; -.
DR KEGG; msm:MSMEG_0434; -.
DR PATRIC; fig|246196.19.peg.430; -.
DR eggNOG; COG0456; Bacteria.
DR OMA; VFDWRDG; -.
DR OrthoDB; 1481620at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Antibiotic resistance; Reference proteome;
KW Transferase.
FT CHAIN 1..210
FT /note="Aminoglycoside 2'-N-acetyltransferase"
FT /id="PRO_0000064411"
FT DOMAIN 21..189
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT BINDING 106..107
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT BINDING 108..110
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT BINDING 115..120
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT BINDING 176..177
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:7CSI"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:7CSI"
FT HELIX 28..41
FT /evidence="ECO:0007829|PDB:7CSI"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:7CSI"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:7CSI"
FT STRAND 76..91
FT /evidence="ECO:0007829|PDB:7CSI"
FT STRAND 97..110
FT /evidence="ECO:0007829|PDB:7CSI"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:7CSI"
FT HELIX 119..134
FT /evidence="ECO:0007829|PDB:7CSI"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:7CSI"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:7CSI"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:7CSI"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:7CSI"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:7CSI"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:7CSI"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:7CSI"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:7CSI"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:7CSI"
SQ SEQUENCE 210 AA; 23168 MW; 002F93B8CE52870B CRC64;
MLTQHVSEAR TRGAIHTARL IHTSDLDQET RDGARRMVIE AFRDPSGDSD FTDDFTDDDW
DHALGGMHAL ISHHGALIAH GAVVQRRLMY RGPDGRGHAL RCGYVEAVAV REDRRGDGLG
TAVLDALEQV IRGAYQIGAL SASDIARPMY IARGWLSWEG PTSVLTPTEG IVRTPEDDRS
LFVLPVDLPD GLELDTAREI TCDWRSGDPW
