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Information on EC 2.7.1.178 - 2-dehydro-3-deoxyglucono/galactono-kinase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q97U29

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EC Tree
IUBMB Comments
The enzyme from the archaeon Sulfolobus solfataricus is involved in glucose and galactose catabolism via the branched variant of the Entner-Doudoroff pathway. It phosphorylates 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate with similar catalytic efficiency. cf. EC 2.7.1.45, 2-dehydro-3-deoxygluconokinase and EC 2.7.1.58, 2-dehydro-3-deoxygalactonokinase.
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Saccharolobus solfataricus
UNIPROT: Q97U29
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The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
2-keto-3-deoxy-D-gluconate kinase, 2-keto-3-deoxygalactonate kinase, 2-keto-3-deoxygluconate kinase, 2-keto-3-deoxyglucononate kinase, HVO_0549, HVO_A0328, KDG kinase, KDGK, KDGK-1, KDGK-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-keto-3-deoxy-D-gluconate kinase
-
2-keto-3-deoxygluconate kinase
-
2-keto-3-deoxygluconate kinase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
show the reaction diagram
(1)
ATP + 2-dehydro-3-deoxy-D-galactonate = ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
show the reaction diagram
(2)
SYSTEMATIC NAME
IUBMB Comments
ATP:2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-D-galactonate 6-phosphotransferase
The enzyme from the archaeon Sulfolobus solfataricus is involved in glucose and galactose catabolism via the branched variant of the Entner-Doudoroff pathway. It phosphorylates 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate with similar catalytic efficiency. cf. EC 2.7.1.45, 2-dehydro-3-deoxygluconokinase and EC 2.7.1.58, 2-dehydro-3-deoxygalactonokinase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-D-galactonate 6-phosphate
show the reaction diagram
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
show the reaction diagram
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
show the reaction diagram
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
show the reaction diagram
additional information
?
-
no activity with 2-dehydro-D-gluconate or 5-dehydro-D-gluconate
-
-
?
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 + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-D-galactonate 6-phosphate
show the reaction diagram
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
show the reaction diagram
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
show the reaction diagram
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
show the reaction diagram
a key enzyme in the semiphosphorylative Entner-Doudoroff pathway in archaea
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.1
2-dehydro-3-deoxy-D-galactonate
pH 7.5, 60°C
0.14 - 3.6
2-dehydro-3-deoxy-D-gluconate
2.8
ATP
pH 7.5, 60°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.4
2-dehydro-3-deoxy-D-galactonate
pH 7.5, 60°C
5 - 60.8
2-dehydro-3-deoxy-D-gluconate
3.8
ATP
pH 7.5, 60°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7
2-dehydro-3-deoxy-D-galactonate
pH 7.5, 60°C
1.4 - 434
2-dehydro-3-deoxy-D-gluconate
1.4
ATP
pH 7.5, 60°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1
calculated from sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
a 2-keto-3-deoxygluconate kinase deletion strain reveals no difference in glycolytic growth compared with the reference strain
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34874
2 * 34874, calculated from sequence
34875
x * 34875, calculated from sequence
37513
x * 37513, mass spectrometric analysis
43000
2 * 43000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method, crystallized in 0.1 M sodium acetate pH 4.1 and 1.4 M NaCl. The crystal structure of apoenzyme is solved by molecular replacement to a resolution of 2.0 A and a ternary complex with 2-dehydro-3-deoxygluconate and an ATP analogue is resolved at 2.1 A. The complex suggests that the structural basis for the enzyme’s ability to phosphorylate 2-oxo-3-deoxygluconate and 2-dehydro-3-deoxygalactonate is derived from a subtle repositioning of residues that are conserved in homologous nonpromiscuous kinases
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
produced as inclusion bodies in Escherichia coli when polyhistidine is used as a fusion tag. To reduce inclusion body formation in Escherichia coli, the enzyme is fused with three partners, thioredoxin, glutathione-S-transferase, and N-utilization substance A. With the use of fusion-partners, the solubility of the archaeal protein is remarkably enhanced, and the soluble fraction of the recombinant protein is increased in this order: thioredoxin > glutathione-S-transferase > N-utilization substance A. In the case of recombinant enzyme, the enzyme activity of the Trx-fused protein is 200-fold higher than that of the polyhistidine-fusion protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, S.; Lee, S.B.
Characterization of Sulfolobus solfataricus 2-keto-3-deoxy-D-gluconate kinase in the modified Entner-Doudoroff pathway
Biosci. Biotechnol. Biochem.
70
1308-1316
2006
Saccharolobus solfataricus (Q97U29), Saccharolobus solfataricus P2 (Q97U29)
Manually annotated by BRENDA team
Kim, S.; Lee, S.B.
Soluble expression of archaeal proteins in Escherichia coli by using fusion-partners
Protein Expr. Purif.
62
116-119
2008
Saccharolobus solfataricus (Q97U29)
Manually annotated by BRENDA team
Potter, J.A.; Kerou, M.; Lamble, H.J.; Bull, S.D.; Hough, D.W.; Danson, M.J.; Taylor, G.L.
The structure of Sulfolobus solfataricus 2-keto-3-deoxygluconate kinase
Acta Crystallogr. Sect. D
64
1283-1287
2008
Saccharolobus solfataricus (Q97U29)
Manually annotated by BRENDA team
Lamble, H.J.; Theodossis, A.; Milburn, C.C.; Taylor, G.L.;, Bull, S.D.; Hough, D.W.; Danson, M.J.
Promiscuity in the part-phosphorylative Entner-Doudoroff pathway of the archaeon Sulfolobus solfataricus
FEBS Lett.
579
6865-6869
2005
Saccharolobus solfataricus (Q97U29)
Manually annotated by BRENDA team
Kouril, T.; Wieloch, P.; Reimann, J.; Wagner, M.; Zaparty, M.; Albers, S.V.; Schomburg, D.; Ruoff, P.; Siebers, B.
Unraveling the function of the two Entner-Doudoroff branches in the thermoacidophilic crenarchaeon Sulfolobus solfataricus P2
FEBS J.
280
1126-1138
2013
Saccharolobus solfataricus, Saccharolobus solfataricus (Q97U29), Saccharolobus solfataricus P2, Saccharolobus solfataricus P2 (Q97U29)
Manually annotated by BRENDA team