ID   AAC3_SERMA              Reviewed;         269 AA.
AC   Q01515;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-MAY-2023, entry version 65.
DE   RecName: Full=Aminoglycoside N(3)-acetyltransferase III;
DE            EC=2.3.1.81;
DE   AltName: Full=ACC(3)-III;
DE   AltName: Full=Aminocyclitol 3-N-acetyltransferase type III;
DE   AltName: Full=Gentamicin-(3)-N-acetyl-transferase;
GN   Name=aac3-Vb;
OS   Serratia marcescens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=82041944;
RX   PubMed=1444303; DOI=10.1128/aac.36.10.2222;
RA   Rather P.N., Mierzwa R., Hare R.S., Miller G.H., Shaw K.J.;
RT   "Cloning and DNA sequence analysis of an aac(3)-Vb gene from Serratia
RT   marcescens.";
RL   Antimicrob. Agents Chemother. 36:2222-2227(1992).
CC   -!- FUNCTION: Resistance to antibiotics containing the 2-deoxy-streptamine
CC       ring including gentamicin, kanamycin, tobramycin, neomycin and
CC       apramycin.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-deoxystreptamine antibiotic + acetyl-CoA = an N(3')-
CC         acetyl-2-deoxystreptamine antibiotic + CoA + H(+);
CC         Xref=Rhea:RHEA:12665, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57921, ChEBI:CHEBI:77452; EC=2.3.1.81;
CC   -!- SIMILARITY: Belongs to the antibiotic N-acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; M97172; AAA26548.1; -; Genomic_DNA.
DR   PIR; A48906; A48906.
DR   RefSeq; WP_033147097.1; NG_047249.1.
DR   PDB; 7LAO; X-ray; 1.92 A; A=1-269.
DR   PDBsum; 7LAO; -.
DR   AlphaFoldDB; Q01515; -.
DR   SMR; Q01515; -.
DR   KEGG; ag:AAA26548; -.
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; IPR003679; Amioglycoside_AcTrfase.
DR   InterPro; IPR028345; Antibiotic_NAT-like.
DR   PANTHER; PTHR11104; AMINOGLYCOSIDE N3-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR11104:SF0; SPBETA PROPHAGE-DERIVED AMINOGLYCOSIDE N(3')-ACETYLTRANSFERASE-LIKE PROTEIN YOKD; 1.
DR   Pfam; PF02522; Antibiotic_NAT; 1.
DR   SUPFAM; SSF110710; TTHA0583/YokD-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Antibiotic resistance; Transferase.
FT   CHAIN           1..269
FT                   /note="Aminoglycoside N(3)-acetyltransferase III"
FT                   /id="PRO_0000068547"
FT   HELIX           4..14
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   STRAND          21..26
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   HELIX           28..31
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   TURN            35..37
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   HELIX           38..49
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   TURN            50..52
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   STRAND          54..58
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   TURN            88..90
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   HELIX           100..106
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   TURN            116..118
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   STRAND          120..124
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   HELIX           127..131
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   STRAND          139..141
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   HELIX           145..151
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   STRAND          155..160
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   HELIX           163..165
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   HELIX           168..175
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   STRAND          183..190
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   STRAND          194..196
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   STRAND          198..205
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   HELIX           212..215
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   HELIX           222..231
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   STRAND          236..241
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   STRAND          244..250
FT                   /evidence="ECO:0007829|PDB:7LAO"
FT   HELIX           251..266
FT                   /evidence="ECO:0007829|PDB:7LAO"
SQ   SEQUENCE   269 AA;  28801 MW;  03C191289479400D CRC64;
     MNTIESITAD LHGLGVRPGD LIMVHASLKA VGPVEGGAAS VVSALRAAVG SAGTLMGYAS
     WDRSPYEETL NGARMDEELR RRWPPFDLAT SGTYPGFGLL NRFLLEAPDA RRSAHPDASM
     VAVGPLAATL TEPHRLGQAL GEGSPLERFV GHGGKVLLLG APLDSVTVLH YAEAIAPIPN
     KRRVTYEMPM LGPDGRVRWE LAEDFDSNGI LDCFAVDGKP DAVETIAKAY VELGRHREGI
     VGRAPSYLFE AQDIVSFGVT YLEQHFGAP
//