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Information on EC 3.6.5.2 - small monomeric GTPase

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EC Tree
IUBMB Comments
A family of about 50 enzymes with a molecular mass of 21 kDa that are distantly related to the alpha-subunit of heterotrimeric G-protein GTPase (EC 3.6.5.1). They are involved in cell-growth regulation (Ras subfamily), membrane vesicle traffic and uncoating (Rab and ARF subfamilies), nuclear protein import (Ran subfamily) and organization of the cytoskeleton (Rho and Rac subfamilies).
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This record set is specific for:
UNIPROT: Q9SSX0
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
k-ras, cdc42, h-ras, small gtpase, ef-tu, rho gtpase, rab11, rab3a, rab27a, rap1a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Rho-type small GTPase
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small GTPase
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GTP-phosphohydrolase
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GTPase
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guanine triphosphatase
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guanosine 5'-triphosphatase
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guanosine triphosphatase
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ribosomal GTPase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
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SYSTEMATIC NAME
IUBMB Comments
GTP phosphohydrolase (cell-regulating)
A family of about 50 enzymes with a molecular mass of 21 kDa that are distantly related to the alpha-subunit of heterotrimeric G-protein GTPase (EC 3.6.5.1). They are involved in cell-growth regulation (Ras subfamily), membrane vesicle traffic and uncoating (Rab and ARF subfamilies), nuclear protein import (Ran subfamily) and organization of the cytoskeleton (Rho and Rac subfamilies).
CAS REGISTRY NUMBER
COMMENTARY hide
9059-32-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
show the reaction diagram
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?
additional information
?
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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
GTP + H2O
GDP + phosphate
show the reaction diagram
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-
-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
Rac/Rop proteins are Rho-type small GTPases that act as molecular switches in plants. They are key components in many major plant signaling pathways, such as innate immunity, pollen tube growth, and root hair formation
physiological function
Rac/Rop protein OsRac1 plays an important role in regulating the production of reactive oxygen species by the NADPH oxidase OsRbohB during innate immunity. Direct OsRac1-OsRbohB interactions activate NADPH oxidase in plants
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RAC1_ORYSJ
214
0
23717
Swiss-Prot
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant GST-tagged OsRac1 complexed with non-hydrolyzable GTP analogue guanosine 5'-(beta,gamma-imido)triphosphate, sitting-drop vapor-diffusion method, mixing of 0.007 ml of 4 mg/ml protein with 0.007 ml of reservoir solution containing 100mM MES, pH 6.0, and 10-30% PEG 6000, 25% v/v glycerol as a cryoprotectant, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C32S/Q68L
design OsRac1 mutants that display reduced binding to the NADPH oxidase OsRbohB. Tyr39 and Asp45 substitutions suppress ROS production in rice cells, these residues are critical for interaction with and activation of NADPH oxidase OsRbohB
G19V
the constitutively activated mutant of OsRac1 increases resistance to rice bacterial blight disease and subsequent cell death
G19V/D38A
site-directed mutagenesis, the Switch I mutant shows unaltered binding with OsRbohB(138-313) compared to the wild-type enzyme
G19V/D45A
site-directed mutagenesis, the Switch I mutant shows markedly attenuated binding with OsRbohB(138-313) compared to the wild-type enzyme
G19V/F35A
site-directed mutagenesis, the Switch I mutant shows markedly attenuated binding with OsRbohB(138-313) compared to the wild-type enzyme
G19V/F44A
site-directed mutagenesis, the Switch I mutant shows moderately reduced binding with OsRbohB(138-313) compared to the wild-type enzyme
G19V/I40A
site-directed mutagenesis, the Switch I mutant shows slightly attenuated binding with OsRbohB(138-313) compared to the wild-type enzyme
G19V/P36A
site-directed mutagenesis, the Switch I mutant shows almost unaltered binding with OsRbohB(138-313) compared to the wild-type enzyme
G19V/P41A
site-directed mutagenesis, the Switch I mutant shows slightly attenuated binding with OsRbohB(138-313) compared to the wild-type enzyme
G19V/T37A
site-directed mutagenesis, the Switch I mutant shows slightly attenuated binding with OsRbohB(138-313) compared to the wild-type enzyme
G19V/T42A
site-directed mutagenesis, the Switch I mutant shows markedly attenuated binding with OsRbohB(138-313) compared to the wild-type enzyme
G19V/V43A
site-directed mutagenesis, the Switch I mutant shows moderately reduced binding with OsRbohB(138-313) compared to the wild-type enzyme
G19V/Y39A
site-directed mutagenesis, the Switch I mutant shows markedly attenuated binding with OsRbohB(138-313) compared to the wild-type enzyme
T24N
a dominant-negative mutant of OsRac1 that decrease the resistance reaction to rice bacterial blight disease and subsequent cell death
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally GST-tagged wild-type and mutant enzymes from Escherichia coli Rosetta (DE3) by glutathione affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
OsRac1, DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally GST-tagged wild-type and mutant enzymes in Escherichia coli Rosetta (DE3), transient coexpression of OsRac1 andthe NADPH oxidase OsRbohB in Nicotiana benthamiana leaves enhancing ROS production
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kosami, K.; Ohki, I.; Nagano, M.; Furuita, K.; Sugiki, T.; Kawano, Y.; Kawasaki, T.; Fujiwara, T.; Nakagawa, A.; Shimamoto, K.; Kojima, C.
The crystal structure of the plant small GTPase OsRac1 reveals its mode of binding to NADPH oxidase
J. Biol. Chem.
289
28569-28578
2014
Oryza sativa (Q9SSX0), Oryza sativa
Manually annotated by BRENDA team