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Information on EC 2.7.1.100 - S-methyl-5-thioribose kinase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9C6D2

for references in articles please use BRENDA:EC2.7.1.100
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IUBMB Comments
CTP also acts, but more slowly.
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9C6D2
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
mtr kinase, 5-methylthioribose kinase, methylthioribose kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methylthioribose kinase
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ATP:S-methylthioribose kinase
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kinase, 5-methylthioribose (phosphorylating)
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methylthioribose kinase
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MTR kinase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ATP:S-methyl-5-thio-D-ribose 1-phosphotransferase
CTP also acts, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY hide
68247-56-3
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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
ATP + S-methyl-5-thio-D-ribose
ADP + 5-methyl-5-thio-D-ribose 1-phosphate
show the reaction diagram
ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-D-ribose 1-phosphate
show the reaction diagram
ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-D-ribose 1-phosphate
show the reaction diagram
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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
ATP + S-methyl-5-thio-D-ribose
ADP + 5-methyl-5-thio-D-ribose 1-phosphate
show the reaction diagram
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?
ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-D-ribose 1-phosphate
show the reaction diagram
enzyme is involved in the recycling of methionine through the methylthioadenosine, i.e. MTA, cycle
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?
ATP + S-methyl-5-thio-D-ribose
ADP + S-methyl-5-thio-D-ribose 1-phosphate
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1
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purified recombinant His-tagged enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression of methylthioribose kinase and other enzymes of the yang cycle is phloem-specific
Manually annotated by BRENDA team
both in Arabidopsis and in Plantago, the Yang cycle enzymes are encoded by highly vasculature-specific genes or by genes showing much stronger expression in the vasculature than in nonvascular tissue. There are high expression levels of S-adenosyl methionine decarboxylases in the vasculature of Arabidopsis and Plantago
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MTK_ARATH
420
0
48071
Swiss-Prot
other Location (Reliability: 2)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure determination, 1.9 A resolution, diffraction data and crystallographic refinement statistics, similarity to enzyme structure of Bacillus subtilis, conformation of Gly-rich loop more extended in Arabidopsis thaliana than in bacterial enzyme homologues, different conformations of G-loops and W-loops in Arabidopsis thaliana and Bacillus subtilis enzymes despite of high sequence similarities, significant ATPase activity in the absence of 5-methyl-5-thio-D-ribose suggested, features of the substrate binding site offer opportunities for a simple organic salt of a 5-methyl-5-thio-D-ribose analog to specifically inhibit kinase activity
purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, 0.002 ml of protein solution containing 10 mg/ml protein in 20 mM imidazole, pH 7.6, 2 mM DTT, 1 mM 5-methyl-5-thio-D-ribose and 1 mM ATP-gamma-S, is mixed an equal volume of reservoir solution containing 10% w/v PEG 8000, 0.1 M sodium cacodylate, pH 6.5, and 0.2 M magnesium acetate, equilibration against 0.5 ml reservoir solution, room temperature, 3 days, cryoprotection by soaking in reservoir solution plus 25% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 1.9 A resolution, identification of heavy-atom derivatives
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
insertional mutagenesis results in inability of the plants to grow on methylthioadenosine as asupplemntal sulfur source, knockout plants show unimpaired growth under standard conditions
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified from inclusion bodies, gel filtration
recombinant GST-fusion protein from Escherichia coli by glutathione affinity chromatography, the GST-tag is cleaved off
recombinant refolded His-tagged enzyme from Escherichia coli by centrifugation, nickel affinity chromatography, ultrafiltration and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
expressed in Escherichia coli
expression as His-tagged enzyme in Escherichia coli strain BL21(DE3) in inclusion bodies
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
both in Arabidopsis and in Plantago, the Yang cycle enzymes are encoded by highly vasculature-specific genes or by genes showing much stronger expression in the vasculature than in nonvascular tissue. There are high expression levels of S-adenosyl methionine decarboxylases in the vasculature of Arabidopsis and Plantago
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
solubilization and refolding of His-tagged enzyme from Escherichia coli inclusion bodies by 6 M guanidium hydrochloride, 0.7 M NaCl, and 20 mM imidazole, at pH 8.0, 30 min at 4°C
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ku, S.Y.; Yip, P.; Cornell, K.A.; Riscoe, M.K.; Howell, P.L.
Crystallization and preliminary X-ray analysis of 5'-methylthioribose kinase from Bacillus subtilis and Arabidopsis thaliana
Acta Crystallogr. Sect. D
60
116-119
2004
Arabidopsis thaliana, Bacillus subtilis
Manually annotated by BRENDA team
Sauter, M.; Cornell, K.A.; Beszteri, S.; Rzewuski, G.
Functional analysis of methylthioribose kinase genes in plants
Plant Physiol.
136
4061-4071
2004
Arabidopsis thaliana (Q9C6D2), Oryza sativa (Q7XR61), Oryza sativa
Manually annotated by BRENDA team
Ku, S.Y.; Cornell, K.A.; Howell, P.L.
Structure of Arabidopsis thaliana 5-methylthioribose kinase reveals a more occluded active site than its bacterial homolog
BMC Struct. Biol.
7
70
2007
Arabidopsis thaliana (Q9C6D2), Arabidopsis thaliana
Manually annotated by BRENDA team
Pommerrenig, B.; Feussner, K.; Zierer, W.; Rabinovych, V.; Klebl, F.; Feussner, I.; Sauer, N.
Phloem-specific expression of Yang cycle genes and identification of novel Yang cycle enzymes in Plantago and Arabidopsis
Plant Cell
23
1904-1919
2011
Plantago major (Q1EMM5), Arabidopsis thaliana (Q9C6D2)
Manually annotated by BRENDA team