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ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phosphogalactonate
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
additional information
?
-
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phosphogalactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phosphogalactonate
-
exogenous galactonate catabolism
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phosphogalactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phosphogalactonate
-
exogenous galactonate catabolism
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phosphogalactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phosphogalactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phosphogalactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phosphogalactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phosphogalactonate
-
L-glucitol catabolism
-
?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-gluconate
ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
-
-
-
?
additional information
?
-
-
enzyme only present in galactonate grown cells, can not be detected in glycerol-, gluconate-, or galactose-grown cells
-
-
?
additional information
?
-
-
enzyme only present in galactonate grown cells, can not be detected in glycerol-, gluconate-, or galactose-grown cells
-
-
?
additional information
?
-
-
induced by growth on galactose medium
-
-
?
additional information
?
-
2-dehydro-3-deoxy-D-gluconate is a weak substrate
-
-
?
additional information
?
-
-
2-dehydro-3-deoxy-D-gluconate is a weak substrate
-
-
?
additional information
?
-
-
enzyme only present in galactonate grown cells, can not be detected in glycerol-, gluconate-, or galactose-grown cells
-
-
?
additional information
?
-
-
enzyme only present in galactonate grown cells, can not be detected in glycerol-, gluconate-, or galactose-grown cells
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phosphogalactonate
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phosphogalactonate
-
exogenous galactonate catabolism
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phosphogalactonate
-
exogenous galactonate catabolism
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phosphogalactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phosphogalactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phosphogalactonate
-
-
-
?
ATP + 2-dehydro-3-deoxy-D-galactonate
ADP + 2-dehydro-3-deoxy-6-phosphogalactonate
-
L-glucitol catabolism
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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evolution
the enzyme belongs to the ASKHA (acetate and sugar kinases/hsc70/actin) family of phosphotransferases, ASKHA signature motifs in KDGal kinase, overview
evolution
-
the enzyme belongs to the ASKHA (acetate and sugar kinases/hsc70/actin) family of phosphotransferases, ASKHA signature motifs in KDGal kinase, overview
-
malfunction
growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation
malfunction
the deletion mutant does not grow on D-galactose
malfunction
-
growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation
-
malfunction
-
the deletion mutant does not grow on D-galactose
-
malfunction
-
growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation
-
malfunction
-
the deletion mutant does not grow on D-galactose
-
malfunction
-
growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation
-
malfunction
-
the deletion mutant does not grow on D-galactose
-
malfunction
-
growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation
-
malfunction
-
the deletion mutant does not grow on D-galactose
-
malfunction
-
growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation
-
malfunction
-
the deletion mutant does not grow on D-galactose
-
malfunction
-
growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation
-
malfunction
-
the deletion mutant does not grow on D-galactose
-
malfunction
-
growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation
-
malfunction
-
the deletion mutant does not grow on D-galactose
-
malfunction
-
growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation
-
malfunction
-
the deletion mutant does not grow on D-galactose
-
metabolism
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
the enzyme is part of the De Ley-Doudoroff 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
-
the enzyme is part of the De Ley-Doudoroff pathway
-
metabolism
-
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
-
the enzyme is part of the De Ley-Doudoroff 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
-
the enzyme is part of the De Ley-Doudoroff 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
-
the enzyme is part of the De Ley-Doudoroff 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
-
the enzyme is part of the De Ley-Doudoroff 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
-
the enzyme is part of the De Ley-Doudoroff 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
-
the enzyme is part of the De Ley-Doudoroff 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
-
the enzyme is part of the De Ley-Doudoroff pathway
-
physiological function
the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea
physiological function
-
the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea
-
physiological function
-
the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea
-
physiological function
-
the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea
-
physiological function
-
the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea
-
physiological function
-
the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea
-
physiological function
-
the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea
-
physiological function
-
the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea
-
physiological function
-
the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea
-
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
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
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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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.
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Deacon, J.; Cooper, R.A.
D-Galactonate utilisation by enteric bacteria. The catabolic pathway in Escherichia coli
FEBS Lett.
77
201-205
1977
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Szumilo, T.
Pathway for D-galactonate catabolism in nonpathogenic mycobacteria
J. Bacteriol.
148
368-370
1981
Mycobacterium butyricum
brenda
Stouthamer, A.H.
Glucose and galactose metabolism in Gluconobacter liquefaciens
Biochim. Biophys. Acta
48
484-500
1961
Gluconacetobacter liquefaciens
-
brenda
Brechtel, E.; Huwig, A.; Giffhorn, F.
L-Glucitol catabolism in Stenotrophomonas maltophilia Ac
Appl. Environ. Microbiol.
68
582-587
2002
Stenotrophomonas maltophilia
brenda
Michalska, K.; Cuff, M.E.; Tesar, C.; Feldmann, B.; Joachimiak, A.
Structure of 2-oxo-3-deoxygalactonate kinase from Klebsiella pneumoniae
Acta Crystallogr. Sect. D
67
678-689
2011
Klebsiella pneumoniae (A6TFZ6), Klebsiella pneumoniae, Klebsiella pneumoniae MGH 78578 (A6TFZ6)
brenda
Pickl, A.; Johnsen, U.; Archer, R.; Schnheit, P.
Identification and characterization of 2-keto-3-deoxygluconate kinase and 2-keto-3-deoxygalactonate kinase in the haloarchaeon Haloferax volcanii
FEMS Microbiol. Lett.
361
76-83
2014
Haloferax volcanii (D4GR05), Haloferax volcanii
brenda
Taestensen, J.B.; Johnsen, U.; Reinhardt, A.; Ortjohann, M.; Schoenheit, P.
D-galactose catabolism in archaea operation of the DeLey-Doudoroff pathway in Haloferax volcanii
FEMS Microbiol. Lett.
367
fnaa029
2020
Haloferax volcanii (D4GR05), Haloferax volcanii, Haloferax volcanii NCIMB 2012 (D4GR05), Haloferax volcanii JCM 8879 (D4GR05), Haloferax volcanii H26 (D4GR05), Haloferax volcanii DS2 (D4GR05), Haloferax volcanii DSM 3757 (D4GR05), Haloferax volcanii ATCC 29605 (D4GR05), Haloferax volcanii NBRC 14742 (D4GR05), Haloferax volcanii VKM B-1768 (D4GR05)
brenda