3.6.4.B7: RadA recombinase
This is an abbreviated version!
For detailed information about RadA recombinase, go to the full flat file.
Word Map on EC 3.6.4.B7
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3.6.4.B7
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strand
-
brca2
-
single-stranded
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meiotic
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fork
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checkpoint
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reca
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ssdna
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nucleoprotein
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helicase
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stall
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radiosensitivity
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non-homologous
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dna-damaging
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fanconi
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radiation-induced
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chromatid
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mre11
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h2ax
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interstrand
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end-joining
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recombinases
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chk1
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meiosis-specific
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homology-directed
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olaparib
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dna-pkcs
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fancd2
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restart
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prophase
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synaptonemal
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parpis
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error-free
-
reca-like
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unrepaired
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gamma-h2ax
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dsb-induced
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d-loops
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ctip
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break-induced
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translesion
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holliday
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bard1
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molecular biology
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synthesis
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atr-dependent
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topbp1
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ssdna-binding
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brca1-mutant
-
rucaparib
-
diagnostics
-
analysis
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pharmacology
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xrcc4
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brca1-deficient
- 3.6.4.B7
- strand
- brca2
-
single-stranded
-
meiotic
- fork
-
checkpoint
- reca
- ssdna
- nucleoprotein
- helicase
-
stall
-
radiosensitivity
-
non-homologous
-
dna-damaging
-
fanconi
-
radiation-induced
-
chromatid
- mre11
- h2ax
-
interstrand
-
end-joining
-
recombinases
- chk1
-
meiosis-specific
-
homology-directed
- olaparib
- dna-pkcs
-
fancd2
-
restart
-
prophase
-
synaptonemal
-
parpis
-
error-free
-
reca-like
-
unrepaired
-
gamma-h2ax
-
dsb-induced
-
d-loops
- ctip
-
break-induced
-
translesion
-
holliday
- bard1
- molecular biology
- synthesis
-
atr-dependent
-
topbp1
-
ssdna-binding
-
brca1-mutant
- rucaparib
- diagnostics
- analysis
- pharmacology
- xrcc4
-
brca1-deficient
Reaction
Synonyms
DNA repair and recombination protein, DNA repair protein RAD51 homolog 1, Hvo RadA, MvRadA, Pho RadA, PhoRadA, Rad51, RadA, RadA intein, RadA recombinase, RadA/Sms, RadC1, RadC2, SMS, SSO0250, SsoRadA, SsoRadA recombinase, SsRada
ECTree
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Metals Ions
Metals Ions on EC 3.6.4.B7 - RadA recombinase
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K+
Mg2+ als well as K+ ions are absorbed at the ATPase center. K+ (but not Na+), stimulates the ATP hydrolysis reaction with an apparent dissociation constant of about 40 mM. The strand exchange activity of the wild-type enzyme is also stimulated by potassium with an apparent dissociation constant of 35 mM
KCl
stimulates the ATPase activity in the absence of ssDNA as well as the strand-exchange activity in the presence of AMPPNP
Mg2+
Mn2+
the enzyme requires the presence of bivalent cations, such as Mg2+ and Mn2+
NaCl
20 mM NaCl used in this mixture was found to be optimal for ATP hydrolysis
NH4Cl
stimulates the ATPase activity in the absence of ssDNA as well as the strand-exchange activity in the presence of AMPPNP
RbCl
stimulates the ssDNA-dependent ATPase activity. 1.0 M RbCl does not stimulate the ATPase activity of MmRadA in the absence of DNA
Mg2+
required for ATPase activity. The enzyme contains a secondary Mg2+ site as well as a canonical P-loop and nucleotide-lined primary Mg2+ site. The secondary Mg2+ site is important for modulating the ATPase activity
Mg2+
the enzyme requires the presence of bivalent cations, such as Mg2+ and Mn2+
Mg2+
required. A magnesium ion is observed in all nucleotide-bound structures. It is positioned in the same location in ATP and AMPPNP structures, co-ordinated by the beta- and gamma-phosphate groups and the hydroxyl group of Thr145. In the ADP structure, the Mg2+ ion is shifted slightly towards the beta-phosphate group, it is also co-ordinated by the beta-phosphate and the hydroxyl group of Thr145, in addition to four water molecules. The residue Glu174 likely activates a water molecule for hydrolysis of ATP. Glu174 forms an indirect interaction with the Mg2+ ion via a bridging water molecule. As magnesium is not present in the crystallisation conditions of RadA, the phosphate-bound form also lacks magnesium, but this appears to have little impact on the binding of the phosphate