ID   AAC6_ACIHA              Reviewed;         145 AA.
AC   Q44057;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Aminoglycoside N(6')-acetyltransferase type 1 {ECO:0000303|PubMed:8257129};
DE            EC=2.3.1.82 {ECO:0000269|PubMed:8257129};
DE   AltName: Full=AAC(6')-Ig {ECO:0000303|PubMed:8257129};
DE   AltName: Full=Aminoglycoside resistance protein {ECO:0000303|PubMed:8257129};
OS   Acinetobacter haemolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=29430;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAA21889.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   SUBSTRATE SPECIFICITY.
RC   STRAIN=BM2685 {ECO:0000312|EMBL:AAA21889.1};
RX   PubMed=8257129; DOI=10.1128/aac.37.10.2093;
RA   Lambert T., Gerbaud G., Galimand M., Courvalin P.;
RT   "Characterization of Acinetobacter haemolyticus aac(6')-Ig gene encoding an
RT   aminoglycoside 6'-N-acetyltransferase which modifies amikacin.";
RL   Antimicrob. Agents Chemother. 37:2093-2100(1993).
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       kanamycin, tobramycin and netilmicin. {ECO:0000269|PubMed:8257129}.
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:8257129};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9R381}.
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DR   EMBL; L09246; AAA21889.1; -; Genomic_DNA.
DR   PIR; I39502; I39502.
DR   RefSeq; WP_005081764.1; NZ_UFRR01000003.1.
DR   PDB; 4EVY; X-ray; 1.77 A; A/B=1-145.
DR   PDB; 4F0Y; X-ray; 2.56 A; A/B=1-145.
DR   PDBsum; 4EVY; -.
DR   PDBsum; 4F0Y; -.
DR   AlphaFoldDB; Q44057; -.
DR   SMR; Q44057; -.
DR   STRING; 1331660.L313_2514; -.
DR   KEGG; ag:AAA21889; -.
DR   eggNOG; COG0456; Bacteria.
DR   BRENDA; 2.3.1.82; 102.
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   3D-structure; Acyltransferase; Antibiotic resistance; Transferase.
FT   CHAIN           1..145
FT                   /note="Aminoglycoside N(6')-acetyltransferase type 1"
FT                   /id="PRO_0000416830"
FT   DOMAIN          1..145
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   BINDING         22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         80..82
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         119
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R381"
FT   STRAND          1..5
FT                   /evidence="ECO:0007829|PDB:4EVY"
FT   HELIX           8..10
FT                   /evidence="ECO:0007829|PDB:4EVY"
FT   HELIX           11..21
FT                   /evidence="ECO:0007829|PDB:4EVY"
FT   HELIX           26..37
FT                   /evidence="ECO:0007829|PDB:4EVY"
FT   STRAND          42..49
FT                   /evidence="ECO:0007829|PDB:4EVY"
FT   STRAND          52..62
FT                   /evidence="ECO:0007829|PDB:4EVY"
FT   STRAND          70..82
FT                   /evidence="ECO:0007829|PDB:4EVY"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:4EVY"
FT   HELIX           91..105
FT                   /evidence="ECO:0007829|PDB:4EVY"
FT   STRAND          110..116
FT                   /evidence="ECO:0007829|PDB:4EVY"
FT   HELIX           120..128
FT                   /evidence="ECO:0007829|PDB:4EVY"
FT   STRAND          132..143
FT                   /evidence="ECO:0007829|PDB:4EVY"
SQ   SEQUENCE   145 AA;  16448 MW;  BAE955A9EABFFA40 CRC64;
     MNIKPASEAS LKDWLELRNK LWSDSEASHL QEMHQLLAEK YALQLLAYSD HQAIAMLEAS
     IRFEYVNGTE TSPVGFLEGI YVLPAHRRSG VATMLIRQAE VWAKQFSCTE FASDAALDNV
     ISHAMHRSLG FQETEKVVYF SKKID