Information on EC 3.6.4.B9 - Rad54 translocase

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The expected taxonomic range for this enzyme is: Sulfolobus solfataricus

EC NUMBER
COMMENTARY hide
3.6.4.B9
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
Rad54 translocase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
double-strand DNA
double-strand DNA-dependent ATPase. The protein itself has a low level of ATP hydrolysis activity, which is not increased by the addition of the ssDNA, poly(dA). Stimulation of ATPase activity is obtained using dsDNA [poly(dA)/poly(dT)] as the substrate
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dsDNA
double-strand DNA-dependent ATPase. The protein itself has a low level of ATP hydrolysis activity, which is not increased by the addition of the ssDNA, poly(dA). Stimulation of ATPase activity is obtained using dsDNA [poly(dA)/poly(dT)] as the substrate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 70
50°C: about 80% of maximal activity, 70°C: about 60% of maximal activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
92853
x * 92853, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method at 25°C, crystals of SsoRad54cd in complex with a 25-mer DNA duplex are refined to 3.0 A resolution. 2.0 A resolution structure of crystals of the C-terminal half of SsoRad54cd separately (residues 432–906)
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E563Q
DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is less than 5% of wild-type activity
G722Q
DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 95% of wild-type activity
K700E
DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 40% of wild-type activity
K711E
DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 30% of wild-type activity
K808E
DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 30% of wild-type activity
K872E
DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 35% of wild-type activity
N569I
mutation reduces both DNA-stimulated ATPase activity and DNA binding activity. DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 35% of wild-type activity
Q755A
DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 40% of wild-type activity
R586W
DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 80% of wild-type activity
R788E
DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 10% of wild-type activity
R840E
DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 5% of wild-type activity
R843E
DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 5% of wild-type activity
V850G
DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 5% of wild-type activity
E563Q
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DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is less than 5% of wild-type activity
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K700E
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DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 40% of wild-type activity
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K711E
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DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 30% of wild-type activity
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N569I
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mutation reduces both DNA-stimulated ATPase activity and DNA binding activity. DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 35% of wild-type activity
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R586W
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DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 80% of wild-type activity
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