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ATP + bluensomycin
diphosphate + 3''-adenylylbluensomycin
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
ATP + spectinomycin
diphosphate + adenylylspectinomycin
ATP + streptobiosamine
diphosphate + 3''-adenylylstreptobiosamine
-
degradation product streptomycin
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
ATP + streptomycin
diphosphate + adenylylstreptomycin
ATP + tetracyclin
diphosphate + 3''adenylyltetracyclin
additional information
?
-
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
inactivation of the antibiotic by adenylating the 9-hydroxyl-group
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
inactivation of the antibiotic by adenylating the 9-hydroxyl-group
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + adenylylspectinomycin
-
-
-
?
ATP + spectinomycin
diphosphate + adenylylspectinomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
enzyme leads to resistance, destroys the inhibitory activity of streptomycin
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
enzyme leads to resistance, destroys the inhibitory activity of streptomycin
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
enzyme leads to resistance, destroys the inhibitory activity of streptomycin
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
enzyme leads to resistance, destroys the inhibitory activity of streptomycin
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
important mechanism of streptomycin modification is through ATP-dependent O -adenylation
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
sequential mechanism, ordered substrate binding where ATP binds first and then streptomycin and diphosphate is released prior to formation of AMP-streptomycin
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
bifunctional enzyme, adenylation of aminoglycoside antibiotics takes place at the ANT(3'')-Ii domain, aceylation of aminoglycoside antibiotics takes place at the AAC(6')-domain
-
-
?
ATP + streptomycin
diphosphate + adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + adenylylstreptomycin
-
-
-
?
ATP + tetracyclin
diphosphate + 3''adenylyltetracyclin
-
-
-
?
ATP + tetracyclin
diphosphate + 3''adenylyltetracyclin
-
-
-
?
ATP + tetracyclin
diphosphate + 3''adenylyltetracyclin
-
-
?
additional information
?
-
-
does not adenylate spectinomycin, enzyme might be identical to AAD aminoglycoside 3''-adenylyltransferase
-
-
?
additional information
?
-
-
does not adenylate spectinomycin, enzyme might be identical to AAD aminoglycoside 3''-adenylyltransferase
-
-
?
additional information
?
-
no resistance to ampicillin, chloramphenicol, ciprofloxacin, gentamicin, imipenem, penicillin, quinupristin/dalfopristin, rifampin, teicoplanin, and vancomycin mediated
-
-
?
additional information
?
-
-
ADP, AMP, UTP, GTP, CTP, TTP, dAMP, adenine, adenosine, S-adenosyl methionine, dADP and ADPglucose are ineffective, streptidine cannot be adenylated by the enzyme, kanamycin and neomycin are not adenylated
-
-
?
additional information
?
-
no substrates: kanamycin A, gentamycin, and amikacin
-
-
?
additional information
?
-
no substrates: kanamycin A, gentamycin, and amikacin
-
-
?
additional information
?
-
-
adenyltransferase domain is highly specific for spectinomycin and streptomycin and catalyzes the reaction by a Theorell-Chance kinetic mechanism, where ATP binds to the enzyme prior to the aminoglycoside and the modified antibiotic is the last product to be released
-
-
?
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ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
enzyme leads to resistance, destroys the inhibitory activity of streptomycin
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
enzyme leads to resistance, destroys the inhibitory activity of streptomycin
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
enzyme leads to resistance, destroys the inhibitory activity of streptomycin
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
enzyme leads to resistance, destroys the inhibitory activity of streptomycin
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
important mechanism of streptomycin modification is through ATP-dependent O -adenylation
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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malfunction
enzyme inactivation decreases streptomycin and spectinomycin resistance by 16fold and 2fold, respectively
malfunction
-
enzyme inactivation decreases streptomycin and spectinomycin resistance by 16fold and 2fold, respectively
-
physiological function
-
aminoglycoside 3''-adenylyltransferase confers resistance to streptomycin and spectinomycin
physiological function
-
aminoglycoside 3'-adenyltransferase confers resistance to spectinomycin
physiological function
-
aminoglycoside 3'-adenyltransferase confers resistance to streptomycin and spectinomycin
physiological function
-
aminoglycoside 3'-adenyltransferase confers resistance to streptomycin and spectinomycin
physiological function
-
aminoglycoside adenyltransferase type A confers resistance to streptomycin and spectinomycin
physiological function
-
aminoglycoside adenyltransferase type A confers resistance to streptomycin and spectinomycin
physiological function
-
aminoglycoside adenylyltransferase type aadA1, aadA2, aadA5, aadA7, and aadA23 confers resistance to streptomycin and spectinomycin, type aac3-Id to gentamicin and sisomicin
physiological function
the enzyme supports streptomycin and spectinomycin resistance
physiological function
-
the enzyme supports streptomycin and spectinomycin resistance
physiological function
-
the enzyme supports streptomycin and spectinomycin resistance
physiological function
the enzyme supports streptomycin and spectinomycin resistance
physiological function
-
the enzyme supports streptomycin and spectinomycin resistance
physiological function
-
the enzyme supports streptomycin and spectinomycin resistance
physiological function
-
the enzyme supports streptomycin and spectinomycin resistance
physiological function
-
the enzyme supports streptomycin and spectinomycin resistance
-
physiological function
-
the enzyme supports streptomycin and spectinomycin resistance
-
physiological function
-
the enzyme supports streptomycin and spectinomycin resistance
-
physiological function
-
the enzyme supports streptomycin and spectinomycin resistance
-
physiological function
-
the enzyme supports streptomycin and spectinomycin resistance
-
physiological function
-
the enzyme supports streptomycin and spectinomycin resistance
-
physiological function
-
the enzyme supports streptomycin and spectinomycin resistance
-
physiological function
-
the enzyme supports streptomycin and spectinomycin resistance
-
physiological function
-
the enzyme supports streptomycin and spectinomycin resistance
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Harwood, J.H.; Smith, D.H.
Resistance factor-mediated streptomycin resistance
J. Bacteriol.
97
1262-1271
1969
Escherichia coli
brenda
Kono, M.; Ohmiya, K.; Kanda, T.; Noguchi, N.; O'Hara, K
Purification and characterization of chromosomal streptomycin adenylyltransferase from derivatives of Bacillus subtilis Marburg 168
FEMS Microbiol. Lett.
40
223-228
1987
Bacillus subtilis, Escherichia coli, Bacillus subtilis Marburg168 BD224
-
brenda
Kazama, H.; Kizu, K.; Iwasaki, M.; Hamashima, H.; Sasatsu, M.; Arai, T.
A new gene, aadA2b, encoding an aminoglycoside adenylyltransferase, AAD(3")(9), isolated from integron InC in Pseudomonas aeruginosa
Microbios
86
77-83
1996
Escherichia coli, Pseudomonas aeruginosa (Q59694), Pseudomonas aeruginosa
brenda
Clark, N.C.; Olsvik, O.; Swenson, J.M.; Spiegel, C.A.; Tenover, F.C.
Detection of a streptomycin/spectinomycin adenylyltransferase gene (aadA) in Enterococcus faecalis
Antimicrob. Agents Chemother.
43
157-160
1999
Enterococcus faecalis (Q71UU1)
brenda
Tauch, A.; Goetker, S.; Puehler, A.; Kalinowski, J.; Thierbach, G.
The 27.8-kb R-plasmid pTET3 from Corynebacterium glutamicum encodes the aminoglycoside adenyltransferase gene cassette aadA9 and the regulated tetracycline efflux system Tet 33 flanked by active copies of the widespread insertion sequence IS6100
Plasmid
48
117-129
2002
Corynebacterium glutamicum, Corynebacterium glutamicum LP-6
brenda
Jana, S.; Deb, J.K.
Kinetic mechanism of streptomycin adenylyltransferase from a recombinant Escherichia coli
Biotechnol. Lett.
27
519-524
2005
Escherichia coli
brenda
Jana, S.; Karan, G.; Deb, J.K.
Purification of streptomycin adenylyltransferase from a recombinant Escherichia coli
Protein Expr. Purif.
40
86-90
2005
Escherichia coli
brenda
Kim, C.; Hesek, D.; Zajicek, J.; Vakulenko, S.B.; Mobashery, S.
Characterization of the bifunctional aminoglycoside-modifying enzyme ANT(3)-Ii/AAC(6)-IId from Serratia marcescens
Biochemistry
45
8368-8377
2006
Serratia marcescens
brenda
Jana, S.; Chaudhuri, T.K.; Deb, J.K.
Effects of guanidine hydrochloride on the conformation and enzyme activity of streptomycin adenylyltransferase monitored by circular dichroism and fluorescence spectroscopy
Biochemistry (Moscow)
71
1230-1237
2006
Escherichia coli
brenda
Chen, Y.G.; Qu, T.T.; Yu, Y.S.; Zhou, J.Y.; Li, L.J.
Insertion sequence ISEcp1-like element connected with a novel aph(2) allele [aph(2)-Ie] conferring high-level gentamicin resistance and a novel streptomycin adenylyltransferase gene in Enterococcus
J. Med. Microbiol.
55
1521-1525
2006
Enterococcus casseliflavus (Q58M14), Enterococcus casseliflavus HZ95 (Q58M14), Enterococcus casseliflavus HZ95
brenda
Ahmed, A.M.; Younis, E.E.; Ishida, Y.; Shimamoto, T.
Genetic basis of multidrug resistance in Salmonella enterica serovars Enteritidis and Typhimurium isolated from diarrheic calves in Egypt
Acta Trop.
111
144-149
2009
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Enteritidis
brenda
Ajiboye, R.M.; Solberg, O.D.; Lee, B.M.; Raphael, E.; Debroy, C.; Riley, L.W.
Global spread of mobile antimicrobial drug resistance determinants in human and animal Escherichia coli and Salmonella strains causing community-acquired infections
Clin. Infect. Dis.
49
365-371
2009
Salmonella enterica subsp. enterica serovar Typhimurium, Escherichia coli (B6ECG5), Escherichia coli (B7TR24), Escherichia coli (Q51348), Escherichia coli (Q5DUC3), Escherichia coli (Q5UNL3), Escherichia coli (Q79JG0), Escherichia coli (Q9F7C0), Escherichia coli (Q9L799), Escherichia coli (Q9R3A9), Escherichia coli
brenda
Mathew, A.G.; Liamthong, S.; Lin, J.; Hong, Y.
Evidence of class 1 integron transfer between Escherichia coli and Salmonella spp. on livestock farms
Foodborne Pathog. Dis.
6
959-964
2009
Escherichia coli, Salmonella
brenda
Randhawa, G.J.; Chhabra, R.; Singh, M.
Multiplex PCR-based simultaneous amplification of selectable marker and reporter genes for the screening of genetically modified crops
J. Agric. Food Chem.
57
5167-5172
2009
Gossypium hirsutum
brenda
Singh, A.K.; Verma, S.S.; Bansal, K.C.
Plastid transformation in eggplant (Solanum melongena L.)
Transgenic Res.
19
113-119
2010
Escherichia coli
brenda
Ahmed, A.M.; Younis, E.E.; Osman, S.A.; Ishida, Y.; El-Khodery, S.A.; Shimamoto, T.
Genetic analysis of antimicrobial resistance in Escherichia coli isolated from diarrheic neonatal calves
Vet. Microbiol.
136
397-402
2009
Escherichia coli
brenda
Shahi, S.K.; Singh, V.K.; Kumar, A.; Gupta, S.K.; Singh, S.K.
Interaction of dihydrofolate reductase and aminoglycoside adenyltransferase enzyme from Klebsiella pneumoniae multidrug resistant strain DF12SA with clindamycin: a molecular modelling and docking study
J. Mol. Model.
19
973-983
2013
Klebsiella pneumoniae (P08881), Klebsiella pneumoniae
brenda
Chen, Y.; Naesvall, J.; Wu, S.; Andersson, D.I.; Selmer, M.
Structure of AadA from Salmonella enterica: a monomeric aminoglycoside (3)(9) adenyltransferase
Acta Crystallogr. Sect. D
71
2267-2277
2015
Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZPX9)
brenda
Papadovasilaki, M.; Oberthr, D.; Gessmann, R.; Sarrou, I.; Betzel, C.; Scoulica, E.Petratos, K.
Biophysical and enzymatic properties of aminoglycoside adenylyltransferase AadA6 from Pseudomonas aeruginosa
Biochem. Biophys. Rep.
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152-157
2015
Pseudomonas aeruginosa (Q9RGC2), Pseudomonas aeruginosa Ps100 (Q9RGC2)
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Stern, A.L.; Van der Verren, S.E.; Kanchugal P, S.; Naesvall, J.; Gutierrez-de-Teran, H.; Selmer, M.
Structural mechanism of AadA, a dual-specificity aminoglycoside adenylyltransferase from Salmonella enterica
J. Biol. Chem.
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2018
Salmonella enterica
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Prabhu, D.; Rajamanikandan, S.; Saritha, P.; Jeyakanthan, J.
Evolutionary significance and functional characterization of streptomycin adenylyltransferase from Serratia marcescens
J. Biomol. Struct. Dyn.
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4418-4431
2020
Serratia marcescens
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Prabhu, D.; Vidhyavathi, R.; Jeyakanthan, J.
Computational identification of potent inhibitors for streptomycin 3 -adenylyltransferase of Serratia marcescens
Microb. Pathog.
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Serratia marcescens
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Zhang, G.; Leclercq, S.O.; Tian, J.; Wang, C.; Yahara, K.; Ai, G.; Liu, S.; Feng, J.
A new subclass of intrinsic aminoglycoside nucleotidyltransferases, ANT(3'')-II, is horizontally transferred among Acinetobacter spp. by homologous recombination
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Acinetobacter baumannii, Acinetobacter baumannii (D0CEM6), Acinetobacter baumannii (Q2FD58), Acinetobacter baumannii ATCC 17978 (Q2FD58), Acinetobacter baumannii ATCC 19606 (D0CEM6), Acinetobacter baumannii AYE, Acinetobacter gyllenbergii, Acinetobacter gyllenbergii NIPH 230, Acinetobacter junii, Acinetobacter junii CIP 64.5, Acinetobacter parvus, Acinetobacter parvus CIP 108168, Acinetobacter pittii, Acinetobacter pittii CIP 70.29, Acinetobacter pittii PHEA-2, Acinetobacter sp. NIPH 758 (IIb) (N8W714), Acinetobacter ursingii, Acinetobacter ursingii ANC 3649
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