Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + 2-deoxy-D-ribitol
ADP + 2-deoxy-D-ribitol 5-phosphate
-
41% of the activity with 2-deoxy-D-ribose
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
ATP + D-arabinose
?
-
weak activity
-
-
?
ATP + D-arabinose
ADP + D-arabinose 5-phosphate
ATP + D-fructose
ADP + D-fructose 5-phosphate
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
ATP + D-xylose
?
1.06% if the activity with D-ribose
-
-
?
ATP + D-xylose
ADP + D-xylose 5-phosphate
-
-
-
-
?
CTP + D-ribose
CDP + D-ribose 5-phosphate
dATP + D-ribose
dADP + D-ribose 5-phosphate
-
108% of the activity with ATP
-
-
?
dCTP + D-ribose
dCDP + D-ribose 5-phosphate
-
25% of the activity with ATP
-
-
?
dGTP + D-ribose
dGDP + D-ribose 5-phosphate
-
50% of the activity with ATP
-
-
?
GTP + D-ribose
GDP + D-ribose 5-phosphate
-
32% of the activity with ATP
-
-
?
ITP + D-ribose
IDP + D-ribose 5-phosphate
-
37% of the activity with ATP
-
-
?
additional information
?
-
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
-
-
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
-
75% of the activity with D-ribose
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
-
-
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
31% if the activity with D-ribose
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
-
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
-
-
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
-
-
-
-
?
ATP + 2-deoxy-D-ribose
ADP + 2-deoxy-D-ribose 5-phosphate
-
first step in the inducible fermentation pathway for this sugar
-
?
ATP + D-arabinose
ADP + D-arabinose 5-phosphate
-
-
-
-
?
ATP + D-arabinose
ADP + D-arabinose 5-phosphate
0.74% if the activity with D-ribose
-
-
?
ATP + D-arabinose
ADP + D-arabinose 5-phosphate
-
4% if the activity with D-ribose
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
highly specific for ribose phosphorylation
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
the enzyme catalyzes the first step of ribose metabolism
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
the enzyme catalyzes the first step of ribose metabolism
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
-
?
ATP + D-ribose
ADP + D-ribose 5-phosphate
-
-
-
?
CTP + D-ribose
CDP + D-ribose 5-phosphate
-
-
-
-
?
CTP + D-ribose
CDP + D-ribose 5-phosphate
-
18% of the activity with ATP
-
-
?
additional information
?
-
-
mutation of a gene encoding a putative ribokinase leads to reduced salt tolerance under potassium limitation in Bacillus subtilis
-
-
?
additional information
?
-
-
L-ribose and L-arabinose are not substrates for the recombinant enzyme
-
-
?
additional information
?
-
GTP displays activity, but at a level which was two orders of magnitude lower versus ATP
-
-
?
additional information
?
-
-
no significant phosphorylation of D-fructose, D-galactose and D-xylose
-
-
?
additional information
?
-
-
mycobacterial topoisomerase I (TopA) is found to physically interact with ribokinase both in vitro and in vivo. The interaction between ribokinase and topoisomerase I has opposite effects on their respective function. While the interaction between the two proteins inhibits the ability of topoisomerase I to relax supercoiled DNA, it stimulates ribokinase activity
-
-
?
additional information
?
-
-
mycobacterial topoisomerase I (TopA) is found to physically interact with ribokinase both in vitro and in vivo. The interaction between ribokinase and TopA has opposite effects on their respective function. While the interaction between the two proteins inhibits the ability of TopA to relax supercoiled DNA, it stimulates ribokinase activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cu2+
-
can replace Mg2+ in activation, optimal concentration: 10 mM, 20% of the activity with Mg2+
Zn2+
-
can replace Mg2+ in activation, optimal concentration: 1 mM, 27% of the activity with Mg2+
Cd2+
may partly support activity
Cd2+
-
can replace Mg2+ in activation, optimal concentration: 5 mM, 68% of the activity with Mg2+
Co2+
-
-
Co2+
about 60% of the activity with Mn2+
Co2+
the enzyme is dependent on monovalent as well as divalent cations for its catalytic activity. When magnesium is substituted with Co2+ and Mn2+ in the reaction mixture, the ribokinase activity got reduced to 60% and 45% as compared to that with Mg2+
Co2+
-
can replace Mg2+ in activation, optimal concentration: 5 mM, 87% of the activity with Mg2+
Cs+
activates
Cs+
-
activity is strongly dependent on the presence of monovalent cations in the order of decreasing efficiency: K+, NH4+, Cs+
Cs+
-
optimal activity obtained in presence of 0.5 M NH4+ or Cs+
K+
activates
K+
-
activity is strongly dependent on the presence of monovalent cations in the order of decreasing efficiency: K+, NH4+, Cs+
K+
the enzyme is dependent on monovalent as well as divalent cations for its catalytic activity. Among the monovalent cations, K+ shows highest activating effect. The activity drops to 90% and 45% with Cs+ and Na+, respectively, in comparison to K+
K+
monovalent ions such as K+ are able to enhance substrate affinity of Sa239 and activate the reaction catalyzed by Sa239
Mg2+
-
absolute requirement for divalent cations, best satisfied by Mg2+
Mg2+
-
optimum concentration at pH 6.2 of free Mg2+ is 2.5 mM
Mg2+
-
activity is cooperatively enhanced by Mn2+ and Mg2+
Mg2+
about 70% of the activity with Mn2+
Mg2+
-
absolute requirement, optimal ratio of Mg2+ to ATP is 1.5 : 1, higher concentrations inhibit
Mg2+
the enzyme is dependent on monovalent as well as divalent cations for its catalytic activity. When magnesium is substituted with Co2+ and Mn2+ in the reaction mixture, the ribokinase activity got reduced to 60% and 45% as compared to that with Mg2+
Mg2+
-
absolute requirement for divalent cations, best satisfied by Mg2+
Mg2+
-
the change in the ratio from Mg2+ to ATP from 1 : 1 to 2 : 1 gives optimal activity
Mg2+
-
the catalytic reactivity of ribokinase is activated by the divalent cation Mg2+, in the absence of these metal ions, ribokinase loses its catalytic ability
Mn2+
-
can replace Mg2+ in activation
Mn2+
-
activity is cooperatively enhanced by Mn2+ and Mg2+
Mn2+
best activator, optimum concentration 0.1 mM
Mn2+
-
cannot replace Mg2+ in the kinase reaction, 50 mM inhibit
Mn2+
the enzyme is dependent on monovalent as well as divalent cations for its catalytic activity. When magnesium is substituted with Co2+ and Mn2+ in the reaction mixture, the ribokinase activity got reduced to 60% and 45% as compared to that with Mg2+
Mn2+
-
can replace Mg2+ in activation
Mn2+
-
optimal concentration 5 mM, 61% of the activity with Mg2+
NH4+
-
activity is strongly dependent on the presence of monovalent cations in the order of decreasing efficiency: K+, NH4+, Cs+
NH4+
-
optimal activity obtained in presence of 0.5 M NH4+ or Cs+
Ni2+
may partly support activity
Ni2+
-
can replace Mg2+, optimal concentration: 25-30 mM, 31% of the activity with Mg2+
additional information
-
no activity in the absence of divalent metal ions
additional information
no activity in the absence of divalent metal ions
additional information
-
no activity in the absence of divalent metal ions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
33.3
2-deoxy-D-ribitol
-
25°C, pH 7.5
0.035 - 1.8
2-deoxy-D-ribose
0.035
2-deoxy-D-ribose
-
30°C, pH 7
0.1
2-deoxy-D-ribose
-
30°C, pH 7.4
0.1
2-deoxy-D-ribose
-
25°C, pH 7.5
1.8
2-deoxy-D-ribose
-
37°C, pH 7.2
0.029
ATP
wild-type, presence of Mn2+, pH 7.2, 37°C
0.04
ATP
-
30°C, pH 7, in presence of Mg2+
0.045
ATP
pH 8.0, temperature not specified in the publication
0.07
ATP
-
37°C, pH 7.0, in presence of 5 mM phosphate
0.08
ATP
-
37°C, pH 7.0, in presence of 2 mM phosphate
0.1
ATP
-
37°C, pH 7.0, in presence of 1 mM phosphate
0.16
ATP
wild-type, presence of Mg2+, pH 7.2, 37°C
2.19
ATP
pH 8.0, 30°C, 100 mM K+
4.66
ATP
pH 8.0, 30°C, 0 mM K+
5.73
ATP
mutant E202L, presence of Mg2+, pH 7.2, 37°C
7.48
ATP
mutant N199L, presence of Mg2+, pH 7.2, 37°C
0.022
D-ribose
-
30°C, pH 7
0.08
D-ribose
mutant E202L, presence of Mg2+, pH 7.2, 37°C
0.11
D-ribose
-
37°C, pH 7.4, 20 mM phosphate
0.12
D-ribose
mutant N199L, presence of Mg2+, pH 7.2, 37°C
0.12
D-ribose
wild-type, presence of Mg2+, pH 7.2, 37°C
0.15
D-ribose
pH 8.0, temperature not specified in the publication
0.18
D-ribose
-
37°C, pH 7.4
0.21
D-ribose
-
37°C, pH 6.2, 20 mM phosphate
0.22
D-ribose
-
37°C, pH 6.2, 20 mM arsenate
0.23
D-ribose
-
37°C, pH 6.2, 5 mM phosphate
0.26
D-ribose
-
37°C, pH 6.2, 5 mM arsenate
0.27
D-ribose
-
37°C, pH 6.2, 1 mM phosphate
0.296
D-ribose
pH 8.5, 25°C
0.32
D-ribose
-
37°C, pH 6.2, 1 mM arsenate
0.33
D-ribose
-
37°C, pH 6.2, 20 mM vanadate
0.43
D-ribose
-
37°C, pH 6.2, 0.5 mM phosphate or 5 mM vanadate
0.46
D-ribose
-
37°C, pH 6.2, 1 mM vanadate
0.48
D-ribose
-
37°C, pH 6.2, 0.5 mM arsenate
0.65
D-ribose
-
37°C, pH 6.2
2
D-ribose
-
30°C, pH 7.4
2
D-ribose
-
25°C, pH 7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ginsburg, A.
A deoxyribokinase from Lactobacillus plantarum
J. Biol. Chem.
234
481-487
1959
Lactiplantibacillus plantarum
brenda
Agranoff, B.W.; Brady, R.O.
Purification and properties of calf liver ribokinase
J. Biol. Chem.
219
221-229
1956
Bos taurus
brenda
Schimmel, S.D.; Hoffee, P.; Horecker, B.L.
Deoxyribokinase from Salmonella typhimurium. Purification and properties
Arch. Biochem. Biophys.
164
560-570
1974
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Goitein, R.K.; Parsons, S.M.
A rapid assay for ribokinase
Anal. Biochem.
75
660-663
1976
Klebsiella aerogenes
brenda
Sigrell, J.A.; Cameron, A.D.; Jones, T.A.; Mowbray, S.L.
Purification, characterization, and crystallization of Escherichia coli ribokinase
Protein Sci.
6
2474-2476
1997
Escherichia coli
brenda
Sigrell, J.A.; Cameron, A.D.; Jones, T.A.; Mowbray, S.L.
Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 A resolution: insights into a new family of kinase structures
Structure
6
183-193
1998
Escherichia coli
brenda
Sigrell, J.A.; Cameron, A.D.; Mowbray, S.L.
Induced fit on sugar binding activates ribokinase
J. Mol. Biol.
290
1009-1018
1999
Escherichia coli (P0A9J6), Escherichia coli
brenda
Maj, M.C.; Gupta, R.S.
The effect of inorganic phosphate on the activity of bacterial ribokinase
J. Protein Chem.
20
139-144
2001
Escherichia coli
brenda
Andersson, C.E.; Mowbray, S.L.
Activation of ribokinase by monovalent cations
J. Mol. Biol.
315
409-419
2002
Escherichia coli (P0A9J6), Escherichia coli
brenda
Tourneux, L.; Bucurenci, N.; Saveanu, C.; Kaminski, P.A.; Bouzon, M.; Pistotnik, E.; Namane, A.; Marliere, P.; Barzu, O.; De La Sierra, I.L.; Neuhard, J.; Gilles, A.M.
Genetic and biochemical characterization of Salmonella enterica serovar typhi deoxyribokinase
J. Bacteriol.
182
869-873
2000
Salmonella enterica
brenda
Ogbunude, P.O.; Lamour, N.; Barrett, M.P.
Molecular cloning, expression and characterization of ribokinase of Leishmania major
Acta Biochim. Biophys. Sin.
39
462-466
2007
Leishmania major
brenda
Chuvikovsky, D.V.; Esipov, R.S.; Skoblov, Y.S.; Chupova, L.A.; Muravyova, T.I.; Miroshnikov, A.I.; Lapinjoki, S.; Mikhailopulo, I.A.
Ribokinase from E. coli: expression, purification, and substrate specificity
Bioorg. Med. Chem.
14
6327-6332
2006
Escherichia coli
brenda
Park, J.; van Koeverden, P.; Singh, B.; Gupta, R.S.
Identification and characterization of human ribokinase and comparison of its properties with E. coli ribokinase and human adenosine kinase
FEBS Lett.
581
3211-3216
2007
Escherichia coli, Homo sapiens
brenda
Ulanova, D.; Holanova, V.; Prenosilova, L.; Naprstek, J.; Licha, I.
Mutation of a gene encoding a putative ribokinase leads to reduced salt tolerance under potassium limitation in Bacillus subtilis
Folia Microbiol. (Praha)
52
203-208
2007
Bacillus subtilis
brenda
Ogbunude, P.O.; Lamour, N.; Barrett, M.P.
Molecular cloning, expression and characterization of ribokinase of Leishmania major
Acta Biochim. Biophys. Sin. (Shanghai)
39
462-466
2007
Leishmania major
brenda
Park, J.; Gupta, R.S.
Adenosine kinase and ribokinase - the RK family of proteins
Cell. Mol. Life Sci.
65
2875-2896
2008
Arabidopsis thaliana, Bos taurus, Saccharomyces cerevisiae, Burkholderia cepacia, Entamoeba histolytica, Homo sapiens, Leishmania major, Salmonella enterica subsp. enterica serovar Typhimurium, Trypanosoma cruzi, Escherichia coli (P0A9J6)
brenda
Wang, L.; Wang, H.; Ruan, J.; Tian, C.; Sun, B.; Zang, J.
Cloning, purification, crystallization and preliminary crystallographic analysis of a ribokinase from Staphylococcus aureus
Acta Crystallogr. Sect. F
65
574-576
2009
Staphylococcus aureus
brenda
Brinkrolf, K.; Ploeger, S.; Solle, S.; Brune, I.; Nentwich, S.S.; Hueser, A.T.; Kalinowski, J.; Puehler, A.; Tauch, A.
The LacI/GalR family transcriptional regulator UriR negatively controls uridine utilization of Corynebacterium glutamicum by binding to catabolite-responsive element (cre)-like sequences
Microbiology
154
1068-1081
2008
Corynebacterium glutamicum (Q8NQR0), Corynebacterium glutamicum, Corynebacterium glutamicum DSM 20300 (Q8NQR0)
brenda
Yang, Q.; Liu, Y.; Huang, F.; He, Z.G.
Physical and functional interaction between D-ribokinase and topoisomerase I has opposite effects on their respective activity in Mycobacterium smegmatis and Mycobacterium tuberculosis
Arch. Biochem. Biophys.
512
135-142
2011
Mycobacterium tuberculosis, Mycolicibacterium smegmatis
brenda
Kori, L.D.; Hofmann, A.; Patel, B.K.
Expression, purification, crystallization and preliminary X-ray diffraction analysis of a ribokinase from the thermohalophile Halothermothrix orenii
Acta Crystallogr. Sect. F
68
240-243
2012
Halothermothrix orenii (B8CWQ8), Halothermothrix orenii
brenda
Li, J.; Wang, C.; Wu, Y.; Wu, M.; Wang, L.; Wang, Y.; Zang, J.
Crystal structure of Sa239 reveals the structural basis for the activation of ribokinase by monovalent cations
J. Struct. Biol.
177
578-582
2012
Staphylococcus aureus (A0A0H2WZY4), Staphylococcus aureus
brenda
Stepchenko, V.; Seela, F.; Esipov, R.; Miroshnikov, A.; Sokolov, Y.; Mikhailopulo, I.
Enzymatic synthesis of 2-deoxy--d-ribonucleosides of 8-azapurines and 8-aza-7-deazapurines
Synlett
23
1541-1545
2012
Escherichia coli
-
brenda
Paul, R.; Dandopath Patra, M.; Banerjee, R.; Sen, U.
Crystallization and preliminary X-ray analysis of a ribokinase from Vibrio cholerae O395
Acta Crystallogr. Sect. F
70
1098-1102
2014
Vibrio cholerae (A0A0H2UL04), Vibrio cholerae, Vibrio cholerae O395 (A0A0H2UL04), Vibrio cholerae O395
brenda
Quiroga-Roger, D.; Babul, J.; Guixe, V.
Role of monovalent and divalent metal cations in human ribokinase catalysis and regulation
Biometals
28
401-413
2015
Homo sapiens (Q9H477), Homo sapiens
brenda
Gatreddi, S.; Are, S.; Qureshi, I.A.
Ribokinase from Leishmania donovani purification, characterization and X-ray crystallographic analysis
Acta Crystallogr. Sect. F
74
99-104
2018
Leishmania donovani (E9BIX7), Leishmania donovani, Leishmania donovani BPK282A1 (E9BIX7)
brenda
Luo, D.; Wang, L.; Liu, H.; Li, L.; Liao, Y.; Yi, X.; Yan, X.; Wan, K.; Zeng, Y.
Ribokinase screened from T7 phage displayed Mycobacterium tuberculosis genomic DNA library had good potential for the serodiagnosis of tuberculosis
Appl. Microbiol. Biotechnol.
103
5259-5267
2019
Mycobacterium tuberculosis (P71913), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P71913)
brenda
Abramchik, Y.; Timofeev, V.; Muravieva, T.; Esipov, R.; Kuranova, I.
Crystallization and preliminary X-ray diffraction study of recombinant ribokinase from Thermus Species 2.9
Crystallogr. Rep.
61
974-978
2016
Thermus sp. 2.9 (A0A0B0SD75)
-
brenda
Gatreddi, S.; Pillalamarri, V.; Vasudevan, D.; Addlagatta, A.; Qureshi, I.A.
Unraveling structural insights of ribokinase from Leishmania donovani
Int. J. Biol. Macromol.
136
253-265
2019
Leishmania donovani (E9BIX7), Leishmania donovani, Leishmania donovani BPK282A1 (E9BIX7)
brenda
Riggs, J.W.; Rockwell, N.C.; Cavales, P.C.; Callis, J.
Identification of the plant ribokinase and discovery of a role for Arabidopsis ribokinase in nucleoside metabolism
J. Biol. Chem.
291
22572-22582
2016
Arabidopsis thaliana (A1A6H3), Arabidopsis thaliana
brenda