2.7.1.58: 2-dehydro-3-deoxygalactonokinase
This is an abbreviated version!
For detailed information about 2-dehydro-3-deoxygalactonokinase, go to the full flat file.
Word Map on EC 2.7.1.58
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2.7.1.58
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d-galactose
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pneumoniae
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dehydratase
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volcanii
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klebsiella
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haloferax
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haloarchaeon
- 2.7.1.58
- d-galactose
- pneumoniae
- dehydratase
- volcanii
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klebsiella
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haloferax
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haloarchaeon
Reaction
Synonyms
2-keto-3-deoxygalactonate kinase, 2-keto-3-deoxygalactonate kinase (phosphorylating), 2-keto-3-deoxygalactonokinase, 2-keto-3-deoxygluconate kinase, 2-oxo-3-deoxy-D-galactonate kinase, 2-oxo-3-deoxygalactonate kinase, HVO A0328, HVO_A0328, KDGal kinase, KDGalA kinase, KDGK-2, KDGK2
ECTree
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General Information
General Information on EC 2.7.1.58 - 2-dehydro-3-deoxygalactonokinase
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evolution
malfunction
metabolism
physiological function
additional information
the enzyme belongs to the ASKHA (acetate and sugar kinases/hsc70/actin) family of phosphotransferases, ASKHA signature motifs in KDGal kinase, overview
evolution
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the enzyme belongs to the ASKHA (acetate and sugar kinases/hsc70/actin) family of phosphotransferases, ASKHA signature motifs in KDGal kinase, overview
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growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation
malfunction
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growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation
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malfunction
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growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation
-
malfunction
-
growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation
-
malfunction
-
growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation
-
malfunction
-
growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation
-
malfunction
-
growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation
-
malfunction
-
growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation
-
malfunction
-
growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation
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the 2-oxo-3-deoxygalactonate kinase catalyzes the penultimate step of an alternative route of D-galactose assimilation, the so-called De Ley-Doudoroff pathway, in which D-galactose is metabolized into pyruvate and D-glyceraldehyde 3-phosphate in five consecutive reactions carried out by specific enzymes. The pathway involves the phosphorylation of 2-oxo-3-deoxygalactonate to 2-oxo-3-deoxygalactonate 6-phosphate catalyzed by the enzyme with ATP serving as a phosphoryl-group donor. Comparison with other D-galactose metabolic pathways, overview. 2-oxo-3-deoxygalactonate 6-phosphate decomposes into puruvate and D-glyceraldehyde 3-phosphate, both products are utilized by the glycolytic pathway
metabolism
a cluster of genes encoding putative enzymes of the DeLey-Doudoroff pathway for D-galactose degradation including galactose dehydrogenase, galactonate dehydratase, 2-keto-3-deoxygalactonate kinase and 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) aldolase is involved in D-galactose degradation. The transcriptional regulator GacR is an activator of genes of the DeLey-Doudoroff pathway
metabolism
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a cluster of genes encoding putative enzymes of the DeLey-Doudoroff pathway for D-galactose degradation including galactose dehydrogenase, galactonate dehydratase, 2-keto-3-deoxygalactonate kinase and 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) aldolase is involved in D-galactose degradation. The transcriptional regulator GacR is an activator of genes of the DeLey-Doudoroff pathway
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metabolism
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the 2-oxo-3-deoxygalactonate kinase catalyzes the penultimate step of an alternative route of D-galactose assimilation, the so-called De Ley-Doudoroff pathway, in which D-galactose is metabolized into pyruvate and D-glyceraldehyde 3-phosphate in five consecutive reactions carried out by specific enzymes. The pathway involves the phosphorylation of 2-oxo-3-deoxygalactonate to 2-oxo-3-deoxygalactonate 6-phosphate catalyzed by the enzyme with ATP serving as a phosphoryl-group donor. Comparison with other D-galactose metabolic pathways, overview. 2-oxo-3-deoxygalactonate 6-phosphate decomposes into puruvate and D-glyceraldehyde 3-phosphate, both products are utilized by the glycolytic pathway
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metabolism
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a cluster of genes encoding putative enzymes of the DeLey-Doudoroff pathway for D-galactose degradation including galactose dehydrogenase, galactonate dehydratase, 2-keto-3-deoxygalactonate kinase and 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) aldolase is involved in D-galactose degradation. The transcriptional regulator GacR is an activator of genes of the DeLey-Doudoroff pathway
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metabolism
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a cluster of genes encoding putative enzymes of the DeLey-Doudoroff pathway for D-galactose degradation including galactose dehydrogenase, galactonate dehydratase, 2-keto-3-deoxygalactonate kinase and 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) aldolase is involved in D-galactose degradation. The transcriptional regulator GacR is an activator of genes of the DeLey-Doudoroff pathway
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metabolism
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a cluster of genes encoding putative enzymes of the DeLey-Doudoroff pathway for D-galactose degradation including galactose dehydrogenase, galactonate dehydratase, 2-keto-3-deoxygalactonate kinase and 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) aldolase is involved in D-galactose degradation. The transcriptional regulator GacR is an activator of genes of the DeLey-Doudoroff pathway
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metabolism
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a cluster of genes encoding putative enzymes of the DeLey-Doudoroff pathway for D-galactose degradation including galactose dehydrogenase, galactonate dehydratase, 2-keto-3-deoxygalactonate kinase and 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) aldolase is involved in D-galactose degradation. The transcriptional regulator GacR is an activator of genes of the DeLey-Doudoroff pathway
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metabolism
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a cluster of genes encoding putative enzymes of the DeLey-Doudoroff pathway for D-galactose degradation including galactose dehydrogenase, galactonate dehydratase, 2-keto-3-deoxygalactonate kinase and 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) aldolase is involved in D-galactose degradation. The transcriptional regulator GacR is an activator of genes of the DeLey-Doudoroff pathway
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metabolism
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a cluster of genes encoding putative enzymes of the DeLey-Doudoroff pathway for D-galactose degradation including galactose dehydrogenase, galactonate dehydratase, 2-keto-3-deoxygalactonate kinase and 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) aldolase is involved in D-galactose degradation. The transcriptional regulator GacR is an activator of genes of the DeLey-Doudoroff pathway
-
metabolism
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a cluster of genes encoding putative enzymes of the DeLey-Doudoroff pathway for D-galactose degradation including galactose dehydrogenase, galactonate dehydratase, 2-keto-3-deoxygalactonate kinase and 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) aldolase is involved in D-galactose degradation. The transcriptional regulator GacR is an activator of genes of the DeLey-Doudoroff pathway
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the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea
physiological function
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the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea
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physiological function
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the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea
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physiological function
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the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea
-
physiological function
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the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea
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physiological function
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the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea
-
physiological function
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the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea
-
physiological function
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the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea
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physiological function
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the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea
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the putative substrate-binding site is created mostly by the N-terminal domain, substrate binding includes the conserved Tyr78 from loop L6, His141 and Lys143 from L15, as well as Glu119 from the H4 helix, nucleotide-binding site structure, overview
additional information
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the putative substrate-binding site is created mostly by the N-terminal domain, substrate binding includes the conserved Tyr78 from loop L6, His141 and Lys143 from L15, as well as Glu119 from the H4 helix, nucleotide-binding site structure, overview
additional information
-
the putative substrate-binding site is created mostly by the N-terminal domain, substrate binding includes the conserved Tyr78 from loop L6, His141 and Lys143 from L15, as well as Glu119 from the H4 helix, nucleotide-binding site structure, overview
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