AAC2_PROST
ID AAC2_PROST Reviewed; 178 AA.
AC Q52424;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Aminoglycoside 2'-N-acetyltransferase;
DE EC=2.3.1.59 {ECO:0000269|PubMed:8407825};
DE AltName: Full=AAC(2')-Ia;
GN Name=aac;
OS Providencia stuartii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=588;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=SCH75082831A;
RX PubMed=8407825; DOI=10.1128/jb.175.20.6492-6498.1993;
RA Rather P.N., Orosz E., Shaw K.J., Hare R., Miller G.;
RT "Characterization and transcriptional regulation of the 2'-N-
RT acetyltransferase gene from Providencia stuartii.";
RL J. Bacteriol. 175:6492-6498(1993).
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:8407825}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + gentamicin C1a = CoA + H(+) + N(2')-
CC acetylgentamicin C1a; Xref=Rhea:RHEA:24516, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58530,
CC ChEBI:CHEBI:58552; EC=2.3.1.59;
CC Evidence={ECO:0000269|PubMed:8407825};
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; L06156; AAA03550.1; -; Unassigned_RNA.
DR PIR; A49899; A49899.
DR RefSeq; WP_004918308.1; NZ_WLUO01000029.1.
DR PDB; 5US1; X-ray; 2.48 A; A/B/C/D/E/F/G/H/I/J/K/L=1-178.
DR PDB; 6VOU; X-ray; 1.95 A; A/B=1-178.
DR PDB; 6VR2; X-ray; 1.77 A; A/B=1-178.
DR PDB; 6VR3; X-ray; 2.00 A; A/B=1-178.
DR PDB; 6VTA; X-ray; 1.42 A; A/B=1-178.
DR PDB; 7JZS; X-ray; 1.30 A; A=2-178.
DR PDBsum; 5US1; -.
DR PDBsum; 6VOU; -.
DR PDBsum; 6VR2; -.
DR PDBsum; 6VR3; -.
DR PDBsum; 6VTA; -.
DR PDBsum; 7JZS; -.
DR AlphaFoldDB; Q52424; -.
DR SMR; Q52424; -.
DR STRING; 588.BGK56_19845; -.
DR KEGG; ag:AAA03550; -.
DR OMA; VFDWRDG; -.
DR OrthoDB; 1481620at2; -.
DR GO; GO:0047921; F:aminoglycoside 2'-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 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..178
FT /note="Aminoglycoside 2'-N-acetyltransferase"
FT /id="PRO_0000064413"
FT DOMAIN 8..171
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT BINDING 79..80
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT BINDING 81..83
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT BINDING 88..93
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT BINDING 148..149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WQG9"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:7JZS"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:7JZS"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:7JZS"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:7JZS"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:7JZS"
FT STRAND 43..51
FT /evidence="ECO:0007829|PDB:7JZS"
FT STRAND 54..68
FT /evidence="ECO:0007829|PDB:7JZS"
FT STRAND 71..83
FT /evidence="ECO:0007829|PDB:7JZS"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:7JZS"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:7JZS"
FT HELIX 92..107
FT /evidence="ECO:0007829|PDB:7JZS"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:7JZS"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:7JZS"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:7JZS"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:7JZS"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:7JZS"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:7JZS"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:7JZS"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:7JZS"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:7JZS"
SQ SEQUENCE 178 AA; 20087 MW; A7D72B79AF6A9AC9 CRC64;
MGIEYRSLHT SQLTLSEKEA LYDLLIEGFE GDFSHDDFAH TLGGMHVMAF DQQKLVGHVA
IIQRHMALDN TPISVGYVEA MVVEQSYRRQ GIGRQLMLQT NKIIASCYQL GLLSASDDGQ
KLYHSVGWQI WKGKLFELKQ GSYIRSIEEE GGVMGWKADG EVDFTASLYC DFRGGDQW
