ID   AACC1_PSEAI             Reviewed;         177 AA.
AC   P23181;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Gentamicin 3-N-acetyltransferase;
DE            EC=2.3.1.60;
DE   AltName: Full=AAC(3)-I {ECO:0000303|PubMed:668926};
DE   AltName: Full=Aminoglycoside N(3)-acetyltransferase I;
DE   AltName: Full=Gentamicin acetyltransferase I;
GN   Name=aacC1;
OS   Pseudomonas aeruginosa.
OG   Plasmid R1033.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2549372; DOI=10.1007/bf02464882;
RA   Wohlleben W., Arnold W., Bissonnette L., Pelletier A., Tanguay A.,
RA   Roy P.H., Gamboa G.C., Barry G.F., Aubert E., Davies J., Kagan S.A.;
RT   "On the evolution of Tn21-like multiresistance transposons: sequence
RT   analysis of the gene (aacC1) for gentamicin acetyltransferase-3-I(AAC(3)-
RT   I), another member of the Tn21-based expression cassette.";
RL   Mol. Gen. Genet. 217:202-208(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-21.
RX   PubMed=668926; DOI=10.1016/0014-5793(78)80730-3;
RA   Hsiang M.W., White T.J., Davies J.E.;
RT   "NH2-terminal sequence of the aminoglycoside acetyltransferase (3)-I
RT   mediated by plasmid RIP 135.";
RL   FEBS Lett. 92:97-99(1978).
CC   -!- FUNCTION: Responsible for gentamicin resistance and has a limited
CC       substrate range.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + gentamicin C = CoA + H(+) + N(3)-acetylgentamycin
CC         C; Xref=Rhea:RHEA:14441, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:75616, ChEBI:CHEBI:75617; EC=2.3.1.60;
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DR   EMBL; U12338; AAB60000.1; -; Genomic_DNA.
DR   EMBL; X15852; CAA33850.1; -; Genomic_DNA.
DR   PIR; JQ0299; JQ0299.
DR   AlphaFoldDB; P23181; -.
DR   SMR; P23181; -.
DR   DrugBank; DB01992; Coenzyme A.
DR   DrugBank; DB03566; Spermidine.
DR   KEGG; ag:CAA33850; -.
DR   GO; GO:0046353; F:aminoglycoside 3-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; 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   Acyltransferase; Antibiotic resistance; Direct protein sequencing; Plasmid;
KW   Transferase; Transposable element.
FT   CHAIN           1..177
FT                   /note="Gentamicin 3-N-acetyltransferase"
FT                   /id="PRO_0000068541"
FT   DOMAIN          25..177
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   177 AA;  19442 MW;  B4DA3DBFBBCDC46D CRC64;
     MLRSSNDVTQ QGSRPKTKLG GSSMGIIRTC RLGPDQVKSM RAALDLFGRE FGDVATYSQH
     QPDSDYLGNL LRSKTFIALA AFDQEAVVGA LAAYVLPRFE QPRSEIYIYD LAVSGEHRRQ
     GIATALINLL KHEANALGAY VIYVQADYGD DPAVALYTKL GIREEVMHFD IDPSTAT