ID   AADB2_KLEPN             Reviewed;         177 AA.
AC   P29806;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=2''-aminoglycoside nucleotidyltransferase;
DE            EC=2.7.7.46;
DE   AltName: Full=AAD(2'');
DE   AltName: Full=Gentamicin 2''-nucleotidyltransferase;
DE   AltName: Full=Gentamicin resistance protein;
GN   Name=aadB;
OS   Klebsiella pneumoniae.
OG   Plasmid pLST1000.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Zieg J., Jiang H., McCabe F., O'Brien T.;
RL   Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mediates bacterial resistance to kanamycin, gentamicin,
CC       dibekacin, sisomicin, neomycin and tobramycin by adenylating the 2''-
CC       hydroxyl group of these antibiotics. {ECO:0000250|UniProtKB:P0AE05}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=nucleoside triphosphate + gentamicin = diphosphate + 2''-
CC         nucleotidylgentamicin.; EC=2.7.7.46;
CC         Evidence={ECO:0000250|UniProtKB:P0AE05};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P0AE05};
CC       Note=Binds 2 Mg(2+). {ECO:0000250|UniProtKB:P0AE05};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X64369; CAA45722.1; -; Genomic_DNA.
DR   PIR; S19940; XNKBLS.
DR   RefSeq; WP_000381803.1; NZ_PTFF02000031.1.
DR   AlphaFoldDB; P29806; -.
DR   SMR; P29806; -.
DR   GO; GO:0008871; F:aminoglycoside 2''-nucleotidyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   InterPro; IPR019646; Aminoglyc_AdlTrfase.
DR   Pfam; PF10706; Aminoglyc_resit; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Magnesium; Metal-binding; Nucleotidyltransferase;
KW   Plasmid; Transferase.
FT   CHAIN           1..177
FT                   /note="2''-aminoglycoside nucleotidyltransferase"
FT                   /id="PRO_0000068558"
FT   ACT_SITE        86
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE05"
FT   BINDING         44
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE05"
FT   BINDING         44
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE05"
FT   BINDING         46
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE05"
FT   BINDING         46
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE05"
FT   BINDING         86
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE05"
SQ   SEQUENCE   177 AA;  19861 MW;  F941A0785D77E719 CRC64;
     MDTTQVTLIH QILAAADERN LPLWIGGGWA IDARLGRVTR KHDDIDLTFP GERRGELEAM
     VEMLGGRVTE ELDYGFLAEI GDELLDCEPA WWADEAYEIA EAPQGSCPEA AEGVIAGRPV
     RCNSWEAIIW DYFYYADEVP PVDWPTKHIE SYRLACTSLG AEKVEVLRAA FRSRYAA