2.7.1.45: 2-dehydro-3-deoxygluconokinase
This is an abbreviated version!
For detailed information about 2-dehydro-3-deoxygluconokinase, go to the full flat file.
Word Map on EC 2.7.1.45
-
2.7.1.45
-
sulfolobus
-
entner-doudoroff
-
archaeon
-
thermus
-
solfataricus
-
non-phosphorylative
-
aldolase
-
hyperthermophilic
-
2-keto-3-deoxy-6-phosphogluconate
-
thermoacidophilic
-
haloferax
-
volcanii
-
2-keto-d-gluconate
-
fructosamine
-
nonphosphorylated
-
galacturonate
-
alginate
-
6-kinase
-
haloarchaeon
-
thermotoga
- 2.7.1.45
- sulfolobus
-
entner-doudoroff
- archaeon
- thermus
- solfataricus
-
non-phosphorylative
- aldolase
-
hyperthermophilic
- 2-keto-3-deoxy-6-phosphogluconate
-
thermoacidophilic
-
haloferax
- volcanii
- 2-keto-d-gluconate
-
fructosamine
-
nonphosphorylated
- galacturonate
- alginate
-
6-kinase
-
haloarchaeon
- thermotoga
Reaction
Synonyms
2-dehydrogluconokinase, 2-keto-3-deoxy-D-gluconate kinase, 2-keto-3-deoxy-D-gluconic acid kinase, 2-keto-3-deoxygluconate kinase, 2-keto-3-deoxygluconokinase, 2-ketogluconate kinase, FlKin, HVO_0549, KDG kinase, KDGK, KDGK-1, ketodeoxygluconokinase, KGUK, KGUKCnec, kinase, 2-keto-3-deoxyglucono- (phosphorylating), More, Ta0122, TM0067
ECTree
2.7.1.45 2-dehydro-3-deoxygluconokinaseAdvanced search results
results (
results (General Information
General Information on EC 2.7.1.45 - 2-dehydro-3-deoxygluconokinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
2-keto-3-deoxy-D-gluconate (KDG) kinase and 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase genes, i.e., flkin and flald, are encoded in the assimilating gene cluster in the genome of Flavobacterium sp. strain UMI-01, a member of Bacteroidetes. The amino acid sequences deduced from flkin and flald show low identities with those of corresponding enzymes of Saccharophagus degradans strain 2-40T, a member of Proteobacteria
malfunction
metabolism
physiological function
malfunction
-
deletion of the semiphosphorylative Entner-Doudoroff pathway key enzyme 2-keto-3-deoxygluconate kinase in Sulfolobus solfataricus PBL2025 results in a similar growth phenotype on glucose as substrate compared with the wild-type. In contrast, the mutant shows strongly increased concentrations of nonphosphorylative-Entner-Doudoroff intermediates whereas the hexose and pentose phosphates as well as trehalose are decreased. The results indicate (a) that the nonphosphorylative pathway is able to compensate for the missing semiphosphorylative Entner-Doudoroff branch in glucose catabolism, (b) that in addition to its catabolic function the semiphosphorylative Entner-Doudoroff pathway has an additional although not essential role in providing sugar phosphates for anabolism/gluconeogenesis and (c) that glycerate kinase, with its unusual regulatory properties, seems to play a major role in controlling the flux between the glycolytic nonphosphorylative Entner-Doudoroff and the glycolytic/gluconeogenetic semiphosphorylative Entner-Doudoroff pathway
malfunction
-
deletion of the semiphosphorylative Entner-Doudoroff pathway key enzyme 2-keto-3-deoxygluconate kinase in Sulfolobus solfataricus PBL2025 results in a similar growth phenotype on glucose as substrate compared with the wild-type. In contrast, the mutant shows strongly increased concentrations of nonphosphorylative-Entner-Doudoroff intermediates whereas the hexose and pentose phosphates as well as trehalose are decreased. The results indicate (a) that the nonphosphorylative pathway is able to compensate for the missing semiphosphorylative Entner-Doudoroff branch in glucose catabolism, (b) that in addition to its catabolic function the semiphosphorylative Entner-Doudoroff pathway has an additional although not essential role in providing sugar phosphates for anabolism/gluconeogenesis and (c) that glycerate kinase, with its unusual regulatory properties, seems to play a major role in controlling the flux between the glycolytic nonphosphorylative Entner-Doudoroff and the glycolytic/gluconeogenetic semiphosphorylative Entner-Doudoroff pathway
-
metabolism
the enzyme occupies a central position in the pectin, galacturonate, and xylan catabolic pathways
metabolism
the enzyme is active in alginate degradation. Unsaturated monosaccharide, the end product of alginate lyases, is spontaneously and/or enzymatically converted to an open chain form, DEH, and further converted to 2-keto-3-deoxy-D-gluconate (KDG) by the NAD(P)H-dependent DEH reductase. The KDG is phosphorylated to KDPG by KDG kinase and then split to pyruvate and glyceraldehyde-3-phosphate (GAP) by KDPG aldolase. The alginate-derived pyruvate and GAP are finally metabolized by Kreb's cycle. Alginate-metabolic system of Flavobacterium sp. strain UMI-01, overview
metabolism
-
the enzyme occupies a central position in the pectin, galacturonate, and xylan catabolic pathways
-
physiological function
2-ketogluconate kinase (KGUK) is involved in the glucose and 2-ketogluconate catabolism of several aerobic bacteria, but relatively few bacterial species are able to utilize 2-ketogluconate as the sole carbon source for growth and energy provision
physiological function
the enzyme is active in alginate degradation
