ID   S3AD_KLEPN              Reviewed;         262 AA.
AC   P08881;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 3.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Aminoglycoside (3'') (9) adenylyltransferase;
DE            EC=2.7.7.47;
DE   AltName: Full=Streptomycin 3''-adenylyltransferase;
GN   Name=aadA {ECO:0000303|PubMed:1963948};
OS   Klebsiella pneumoniae.
OG   Plasmid pJHC-MW1, and Plasmid pBP201.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TRANSPOSON=Tn1331;
RX   PubMed=1963948; DOI=10.1016/0147-619x(90)90005-w;
RA   Tolmasky M.E.;
RT   "Sequencing and expression of aadA, bla, and tnpR from the multiresistance
RT   transposon Tn1331.";
RL   Plasmid 24:218-226(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
RC   TRANSPOSON=Tn1331;
RX   PubMed=2841303; DOI=10.1128/jb.170.8.3769-3773.1988;
RA   Nobuta K., Tolmasky M.E., Crosa L.M., Crosa J.H.;
RT   "Sequencing and expression of the 6'-N-acetyltransferase gene of transposon
RT   Tn1331 from Klebsiella pneumoniae.";
RL   J. Bacteriol. 170:3769-3773(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RC   STRAIN=18440; TRANSPOSON=Tn4000;
RX   PubMed=2850441; DOI=10.1111/j.1365-2958.1988.tb00081.x;
RA   Schmidt F.R.J., Nuecken E.J., Henschke R.B.;
RT   "Nucleotide sequence analysis of 2''-aminoglycoside nucleotidyl-transferase
RT   ANT(2'') from Tn4000: its relationship with AAD(3'') and impact on Tn21
RT   evolution.";
RL   Mol. Microbiol. 2:709-717(1988).
RN   [4]
RP   PROBABLE STREPTOMYCIN RESISTANCE.
RC   TRANSPOSON=Tn1331;
RX   PubMed=2830842; DOI=10.1128/aac.31.12.1955;
RA   Tolmasky M.E., Crosa J.H.;
RT   "Tn1331, a novel multiresistance transposon encoding resistance to amikacin
RT   and ampicillin in Klebsiella pneumoniae.";
RL   Antimicrob. Agents Chemother. 31:1955-1960(1987).
CC   -!- FUNCTION: Mediates bacterial resistance to the antibiotics streptomycin
CC       and spectinomycin. {ECO:0000250|UniProtKB:P0AG05,
CC       ECO:0000305|PubMed:2830842}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + streptomycin = 3''-O-adenylylstreptomycin + diphosphate;
CC         Xref=Rhea:RHEA:20245, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58007, ChEBI:CHEBI:58605; EC=2.7.7.47;
CC         Evidence={ECO:0000250|UniProtKB:P0AG05};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + spectinomycin = 9-O-adenylylspectinomycin + diphosphate;
CC         Xref=Rhea:RHEA:63228, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:146260, ChEBI:CHEBI:146261;
CC         Evidence={ECO:0000250|UniProtKB:P0AG05};
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA69750.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
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DR   EMBL; M55547; AAA98405.1; -; Genomic_DNA.
DR   EMBL; X12618; CAA31140.1; -; Genomic_DNA.
DR   EMBL; M21682; AAA69750.1; ALT_SEQ; Genomic_DNA.
DR   PIR; C37392; C37392.
DR   PIR; S04171; S04171.
DR   RefSeq; NP_608308.1; NC_003486.1.
DR   RefSeq; WP_011018350.1; NC_003486.1.
DR   AlphaFoldDB; P08881; -.
DR   SMR; P08881; -.
DR   BRENDA; 2.7.7.47; 2814.
DR   GO; GO:0070566; F:adenylyltransferase activity; IEA:InterPro.
DR   GO; GO:0009012; F:aminoglycoside 3''-adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.460.10; -; 1.
DR   InterPro; IPR024172; AadA/Aad9.
DR   InterPro; IPR025184; DUF4111.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR   Pfam; PF13427; DUF4111; 1.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   PIRSF; PIRSF000819; Streptomycin_3-adenylyltransf; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; ATP-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Plasmid; Transferase; Transposable element.
FT   CHAIN           1..262
FT                   /note="Aminoglycoside (3'') (9) adenylyltransferase"
FT                   /id="PRO_0000068581"
FT   VARIANT         8
FT                   /note="K -> E (in plasmid pBP201)"
FT   VARIANT         15
FT                   /note="E -> Q (in plasmid pBP201)"
SQ   SEQUENCE   262 AA;  29202 MW;  A2EEB44DA6272C85 CRC64;
     MREAVIAKVS TQLSEVVGVI ERHLEPTLLA VHLYGSAVDG GLKPHSDIDL LVTVTVRLDE
     TTRRALINDL LETSASPGES EILRAVEVTI VVHDDIIPWR YPAKRELQFG EWQRNDILAG
     IFEPATIDID LAILLTKARE HSVALVGPAA EELFDPVPEQ DLFEALNETL TLWNSPPDWA
     GDERNVVLTL SRIWYSAVTG KIAPKDVAAD WAMERLPAQY QPVILEARQA YLGQEDRLAS
     RADQLEEFVH YVKGEITKVV GK