Information on EC 2.7.7.47 - streptomycin 3''-adenylyltransferase

Word Map on EC 2.7.7.47
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.7.7.47
-
RECOMMENDED NAME
GeneOntology No.
streptomycin 3''-adenylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + streptomycin = diphosphate + 3''-adenylylstreptomycin
show the reaction diagram
also acts on sprctionomycin
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:streptomycin 3''-adenylyltransferase
Also acts on spectinomycin.
CAS REGISTRY NUMBER
COMMENTARY hide
52660-23-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Marburg168 BD224
-
-
Manually annotated by BRENDA team
Marburg168 BD224
-
-
Manually annotated by BRENDA team
HZ95
SwissProt
Manually annotated by BRENDA team
W4770, aadA nucleotide sequence
SwissProt
Manually annotated by BRENDA team
gene modified crop, GM cotton events MON 531, MON 15985, MON 88913
-
-
Manually annotated by BRENDA team
PAO4141, nucleotide sequence of InC
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + bluensomycin
diphosphate + 3''-adenylylbluensomycin
show the reaction diagram
-
-
-
?
ATP + spectinomycin
diphosphate + 9-adenylylspectinomycin
show the reaction diagram
ATP + streptobiosamine
diphosphate + 3''-adenylylstreptobiosamine
show the reaction diagram
-
degradation product streptomycin
-
?
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
show the reaction diagram
ATP + streptomycin
diphosphate + 9-adenylylstreptomycin
show the reaction diagram
ATP + tetracyclin
diphosphate + 3''adenylyltetracyclin
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + streptomycin
diphosphate + 3''-adenylylstreptomycin
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
ADP, AMP, adenosine, adenine other nucleoside triphosphates or other deoxyadenine-containing compounds cannot replace ATP
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
Ni2+, Co2+, Ca2+, Zn2+ and Mn2+ cannot replace Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9-O-(adenosine-5'-phophoryl)spectinomycin
-
product inhibition of ANT(3'')-Ii domain
AMP-CPP
-
dead-end inhibition of ANT(3'')-Ii domain
clindamycin
residues Phe34, Asp60, Arg63, Gln64, Leu68, Glu87, Thr89, Val90 are responsible for positioning clindamycin into the active site
kanamycin A
-
dead-end inhibition of ANT(3'')-Ii domain
neomycin
-
non-competitive versus streptomycin and uncompetitive versus ATP
tobramycin
-
non-competitive versus streptomycin and uncompetitive versus ATP
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
enhances the degree of streptomycin inactivation
Tris-HCl
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014
ATP
-
kinetic parameter of the ANT(3'')-Ii domain of the enzyme
0.0014
spectinomycin
-
kinetic parameter of the ANT(3'')-Ii domain of the enzyme
0.00008 - 0.0013
streptomycin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
ATP
Serratia marcescens
-
turnover number of ANT(3'')-Ii domain
0.5
spectinomycin
Serratia marcescens
-
turnover number of ANT(3'')-Ii domain
0.6
streptomycin
Serratia marcescens
-
turnover number of ANT(3'')-Ii domain
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.076 - 0.093
9-O-(adenosine-5'-phophoryl)spectinomycin
0.017 - 0.021
AMP-CPP
0.004 - 0.01
kanamycin A
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000046
-
streptomycin
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
7.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
additional information
-
assay is performed at room temperature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2
-
isoelectric focusing
6
-
isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
resistance factor RE130, extrachromosomal genetic element
Manually annotated by BRENDA team
-
periplasmic space
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
-
deduced from open reading frame
49000
-
x * 49000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 49000, SDS-PAGE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
modeling of enzyme structure
to 2.5 A resolution. AadA consists of a nucleotidyltransferase domain and an alpha-helical bundle domain. AadA crystallizes as a monomer. ATP binding has to occur before binding of the aminoglycoside substrate, and ATP binding repositions the two domains for aminoglycoside binding in the interdomain cleft
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
retention of 90% native-like secondary structure at 0.5 M guanidine hydrochloride, loss of 50% and 75% of secondary structure and 35% and 60% of activity at 0.75 M and 1.5 M guanidine hydrochloride, respectively, at 6 M guanidine hydrochloride loss of secondary structure and activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE anion-exchange column and gentamycin affinity column
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
27.8 kb R-plasmid pTET3 gene cassette aadA9, antibiotic resistance region identified in Mycobacterium fortuitum, cloned in Escherichia coli DH5alphaMCR
-
aadA resistence gene transferred vi filter mating from Enterococcus faecalis W4770 to Enterococcus faecalis JH2-2, PCR amplified aadA gene cloned into vector pCRII and transformed into Escherichia coli DH5-alpha
cloned in Escherichia coli BL21
-
gene aadA2B isolated from integron InC as a gene cassette, Escherichia coli cells transformed by electroporation
into the vector pGEM-T for sequencing
streptomycin adenylyltransferase gene isolated from unconjugative plasmids of Enterococcus casseliflavus HZ95 is cloned in Escherichia coli DH5alpha
the plastid expression vector pPRV111A carrying the aadA gene encoding aminoglycoside 3''-adenylyltransferase is used for plastid transformation in Solanum melongena
-
thioredoxin-His6-tagged SMATase fusion protein is produced in a bacterial intracellular expression system mainly in a soluble form
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D182A
mutation reduces the MIC of streptomycin and spectinomycin
D182N
mutation reduces the MIC of streptomycin and spectinomycin
E87A
mutation reduces the MIC of streptomycin and spectinomycin to that of an AadA null strain
E87Q
mutation reduces the MIC of streptomycin and spectinomycin to that of an AadA null strain
K205A
mutation reduces the MIC of streptomycin and spectinomycin
R192A
mutation reduces the MIC of streptomycin and spectinomycin
W112A
mutation reduces the MIC of spectinomycin to that of an AadA null strain and reduces the MIC of streptomycin
W112F
mutation reduces the MIC of spectinomycin to that of an AadA null strain and reduces the MIC of streptomycin
D182A
-
mutation reduces the MIC of streptomycin and spectinomycin
-
D182N
-
mutation reduces the MIC of streptomycin and spectinomycin
-
E87Q
-
mutation reduces the MIC of streptomycin and spectinomycin to that of an AadA null strain
-
K205A
-
mutation reduces the MIC of streptomycin and spectinomycin
-
R192A
-
mutation reduces the MIC of streptomycin and spectinomycin
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
aminoglycoside 3''-adenylyltransferase confers resistance to streptomycin and spectinomycin
analysis
-
the developed multiplex PCR assay is useful in verifying the GM status of a sample irrespective of the crop and GM trait
diagnostics
medicine
Show AA Sequence (1149 entries)
Please use the Sequence Search for a specific query.