Information on EC 2.7.7.B22 - transposase

Word Map on EC 2.7.7.B22
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: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
2.7.7.B22
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
transposase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
binds to the ends of a transposon (DNA that moves) and catalyzes the movement of the transposon to another part of the genome by a cut and paste mechanism or a replicative transposition mechanism
show the reaction diagram
-
-
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
His16, Asp59, and His60 play important roles in maintaining the metal binding site
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 16379, calculated from sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method at 24°C, crystal structure of the enzyme in both Mn2+-bound and Mn2+-free forms
hanging-drop vapour-diffusion method, crystallized at 24°C using a reservoir solution consisting of 100 mM Na HEPES pH 7.5 and 20%(v/v) ethanol. X-ray diffraction data are collected to 1.78 A. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 65.00, b = 34.07, c = 121.58 A, alpha = 90, beta = 100.20, gamma = 90
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpressed in intact form in Escherichia coli