ID   AAC2_MYCTO              Reviewed;         181 AA.
AC   P9WQG8; L0T655; P0A5N0; P72033; P95219;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Aminoglycoside 2'-N-acetyltransferase;
DE            EC=2.3.1.-;
DE   AltName: Full=AAC(2')-Ic;
GN   Name=aac; OrderedLocusNames=MT0275;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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 (By similarity).
CC       {ECO:0000250|UniProtKB:P94968}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WQG9}.
CC   -!- SIMILARITY: Belongs to the AAC(2')-I acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK44495.1; -; Genomic_DNA.
DR   PIR; A70627; A70627.
DR   RefSeq; WP_003899880.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQG8; -.
DR   SMR; P9WQG8; -.
DR   EnsemblBacteria; AAK44495; AAK44495; MT0275.
DR   GeneID; 45424234; -.
DR   KEGG; mtc:MT0275; -.
DR   PATRIC; fig|83331.31.peg.293; -.
DR   HOGENOM; CLU_106718_0_0_11; -.
DR   Proteomes; UP000001020; 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   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Antibiotic resistance; Transferase.
FT   CHAIN           1..181
FT                   /note="Aminoglycoside 2'-N-acetyltransferase"
FT                   /id="PRO_0000426777"
FT   DOMAIN          11..162
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   BINDING         35
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT   BINDING         82..83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT   BINDING         84..86
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT   BINDING         91..96
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT   BINDING         151..152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQG9"
SQ   SEQUENCE   181 AA;  20038 MW;  A5F553E9DCBF1F0A CRC64;
     MHTQVHTARL VHTADLDSET RQDIRQMVTG AFAGDFTETD WEHTLGGMHA LIWHHGAIIA
     HAAVIQRRLI YRGNALRCGY VEGVAVRADW RGQRLVSALL DAVEQVMRGA YQLGALSSSA
     RARRLYASRG WLPWHGPTSV LAPTGPVRTP DDDGTVFVLP IDISLDTSAE LMCDWRAGDV
     W