AADB_ECOLX
ID AADB_ECOLX Reviewed; 177 AA.
AC P0AE04; P08880; P10019;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 60.
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 Escherichia coli.
OG Plasmid pDGO100, and Plasmid IncQ pIE723.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pDGO100;
RX PubMed=3024112; DOI=10.1093/nar/14.21.8625;
RA Cameron F.H., Groot Obbink D.J., Ackerman V.P., Hall R.M.;
RT "Nucleotide sequence of the AAD(2'') aminoglycoside adenylyltransferase
RT determinant aadB. Evolutionary relationship of this region with those
RT surrounding aadA in R538-1 and dhfrII in R388.";
RL Nucleic Acids Res. 14:8625-8635(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O147:K88 / IE1003; PLASMID=IncQ pIE723;
RA Tietze E.;
RT "Nucleotide sequence and expression of a gentamicin resistance gene
RT cassette from the IncQ plasmid pIE723.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates bacterial resistance to kanamycin, gentamicin and
CC tobramycin by adenylating the 2''-hydroxyl group of these antibiotics.
CC {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 -!- SEQUENCE CAUTION:
CC Sequence=CAA28209.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L06418; AAA92745.1; -; Genomic_DNA.
DR EMBL; U14415; AAA85811.1; -; Genomic_DNA.
DR EMBL; X04555; CAA28209.1; ALT_INIT; Genomic_DNA.
DR EMBL; M86913; AAA72105.1; -; Genomic_DNA.
DR EMBL; Z47410; CAA87463.1; -; Genomic_DNA.
DR PIR; A25536; XNECAD.
DR RefSeq; WP_000381802.1; NZ_WUBH01000061.1.
DR AlphaFoldDB; P0AE04; -.
DR SMR; P0AE04; -.
DR GeneID; 67369350; -.
DR KEGG; ag:CAA28209; -.
DR OrthoDB; 1551670at2; -.
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; Transposable element.
FT CHAIN 1..177
FT /note="2''-aminoglycoside nucleotidyltransferase"
FT /id="PRO_0000068556"
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; 19873 MW; 9A084D96AE99F2F1 CRC64;
MDTTQVTLIH KILAAADERN LPLWIGGGWA IDARLGRVTR KHDDIDLTFP GERRGELEAI
VEMLGGRVME ELDYGFLAEI GDELLDCEPA WWADEAYEIA EAPQGSCPEA AEGVIAGRPV
RCNSWEAIIW DYFYYADEVP PVDWPTKHIE SYRLACTSLG AEKVEVLRAA FRSRYAA
