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Information on EC 3.6.4.B7 - RadA recombinase

for references in articles please use BRENDA:EC3.6.4.B7
preliminary BRENDA-supplied EC number
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UNIPROT: O74036
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Word Map
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Reaction Schemes
Synonyms
rad51, rada/sms, ssorada, dna repair protein rad51 homolog 1, rada recombinase, rada intein, radc1, dna repair and recombination protein, mvrada, radc2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
?
-
The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
-
-
?
NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ssDNA
ATPase activity of RadA is drastically stimulated by ssDNA and to a lesser extent by dsDNA. The activity increases linearly with ssDNA concentration until a saturation plateau, at which the apparent binding stoichiometry is 3 nucleotides for 1 RadA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017 - 0.0345
ATP
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the RecA/RadA family of recombinase proteins, including RecA proteins of bacteria, RadAs in archaea, Rad51 and DMC1 proteins in Eukaryotes. Archaea and eukaryotes encode RadA/Rad51 paralogues, such as Rad55/57 in yeast, Rad51B/C/D, Xrcc2 and Xrcc3 in mammals, and RadB, RadC in Archaea, which facilitate homologous recombination by interacting with RadA/Rad51 recombinases. Archaeal RadA and eukaryotic Rad51 proteins show high amino acid sequence identities to each other (over 40%) but they are more distantly related to bacterial RecA proteins, exhibiting about 20% sequence identity. Archaeal and eukaryotic recombinases are also more closely related to each other at protein domain structure. RadA paralogues represent another major group of AAA + ATPases involved in DNA damage repair in Archaea
metabolism
nanobiomotors perform various important functions in the cell, and they also emerge as potential vehicle for drug delivery. The proteins employ conserved ATPase domains to convert chemical energy to mechanical work and motion. Some are active during DNA damage repair. All nanobiomotors contain an ATPase domain that adopts RecA fold structure, characteristic for RecA/RadA family proteins, structural analyses of archaeal nucleic acid biomotors and the molecular mechanisms of how ATP binding and hydrolysis promote the conformation change that drives mechanical motion
physiological function
additional information
the ring and right-handed filament structures of RadAs, domain structure and organization, overview. In the absence of ATP, the Walker motifs adopt a conformation to hold the ATP-binding site open and do not interact with the adjacent ATPase domain
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RADA_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
349
0
38399
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38400
x * 38400, SDS-PAGE, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 38400, SDS-PAGE, calculated from sequence
oligomer
stable selfassociation of the RadA proteins
additional information
enzyme domain organization, structure comparisons, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis, PDB ID 1PZN
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of radA might be constitutive
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
application potential of archaeal nanobiomotors in drug delivery
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Komori, K.; Miyata, T.; DiRuggiero, J.; Holley-Shanks, R.; Hayashi, I.; Cann, I.K.; Mayanagi, K.; Shinagawa, H.; Ishino, Y.
Both RadA and RadB are involved in homologous recombination in Pyrococcus furiosus
J. Biol. Chem.
275
33782-33790
2000
Pyrococcus furiosus (O74036), Pyrococcus furiosus
Manually annotated by BRENDA team
Komori, K.; Miyata, T.; Daiyasu, H.; Toh, H.; Shinagawa, H.; Ishino, aY.
Domain analysis of an archaeal RadA protein for the strand exchange activity
J. Biol. Chem.
275
33791-33797
2000
Pyrococcus furiosus (O74036), Pyrococcus furiosus
Manually annotated by BRENDA team
Han, W.; Shen, Y.; She, Q.
Nanobiomotors of archaeal DNA repair machineries: current research status and application potential
Cell Biosci.
4
32
2014
Archaeoglobus fulgidus, Sulfolobus islandicus, Sulfurisphaera tokodaii, Methanococcus voltae (O73948), Pyrococcus furiosus (O74036), Saccharolobus solfataricus (Q55075), Thermoplasma acidophilum (Q9HJ68), Saccharolobus solfataricus P2 (Q55075), Thermoplasma acidophilum ATCC 25905 (Q9HJ68)
Manually annotated by BRENDA team