EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.376 | overexpression in Haloferax volcanii H1209 | Haloferax volcanii |
2.7.1.58 | gene kdgK1, recombinant overexpression in Haloferax volcanii strain H1209 | Haloferax volcanii |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.376 | 0.32 | - |
NADP+ | pH 8.0, temperature not specified in the publication | Haloferax volcanii | |
1.1.1.376 | 2 | 3 | D-galactose | pH 8.0, temperature not specified in the publication | Haloferax volcanii | |
1.1.1.376 | 35 | - |
L-arabinose | pH 8.0, temperature not specified in the publication | Haloferax volcanii | |
2.7.1.58 | 0.2 | - |
2-dehydro-3-deoxy-D-galactonate | pH and temperature not specified in the publication | Haloferax volcanii | |
2.7.1.58 | 0.3 | - |
ATP | pH and temperature not specified in the publication | Haloferax volcanii | |
2.7.1.58 | 8.8 | - |
2-dehydro-3-deoxy-D-gluconate | pH and temperature not specified in the publication | Haloferax volcanii |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.376 | KCl | maximal activities are obtained at KCl concentrations higher than 1 M | Haloferax volcanii |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.1.1.376 | 76000 | - |
- |
Haloferax volcanii |
2.7.1.58 | 194000 | - |
- |
Haloferax volcanii |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.376 | D-galactose + NADP+ | Haloferax volcanii | the enzyme has an essential function during growth on D-galactose | D-galactono-1,4-lactone + NADPH + H+ | - |
? | |
1.1.1.376 | D-galactose + NADP+ | Haloferax volcanii ATCC 29605 | the enzyme has an essential function during growth on D-galactose | D-galactono-1,4-lactone + NADPH + H+ | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-galactonate | Haloferax volcanii | - |
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-galactonate | Haloferax volcanii NCIMB 2012 | - |
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-galactonate | Haloferax volcanii JCM 8879 | - |
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-galactonate | Haloferax volcanii H26 | - |
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-galactonate | Haloferax volcanii DS2 | - |
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-galactonate | Haloferax volcanii DSM 3757 | - |
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-galactonate | Haloferax volcanii ATCC 29605 | - |
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-galactonate | Haloferax volcanii NBRC 14742 | - |
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-galactonate | Haloferax volcanii VKM B-1768 | - |
ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.376 | Haloferax volcanii | D4GR07 | - |
- |
1.1.1.376 | Haloferax volcanii ATCC 29605 | D4GR07 | - |
- |
2.7.1.58 | Haloferax volcanii | D4GR05 | - |
- |
2.7.1.58 | Haloferax volcanii ATCC 29605 | D4GR05 | - |
- |
2.7.1.58 | Haloferax volcanii DS2 | D4GR05 | - |
- |
2.7.1.58 | Haloferax volcanii DSM 3757 | D4GR05 | - |
- |
2.7.1.58 | Haloferax volcanii H26 | D4GR05 | - |
- |
2.7.1.58 | Haloferax volcanii JCM 8879 | D4GR05 | - |
- |
2.7.1.58 | Haloferax volcanii NBRC 14742 | D4GR05 | - |
- |
2.7.1.58 | Haloferax volcanii NCIMB 2012 | D4GR05 | - |
- |
2.7.1.58 | Haloferax volcanii VKM B-1768 | D4GR05 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.1.376 | - |
Haloferax volcanii |
2.7.1.58 | recombinant enzyme from Haloferax volcanii strain H1209 | Haloferax volcanii |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
2.7.1.58 | culture condition:D-galactose-grown cell | - |
Haloferax volcanii | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.1.1.376 | 323 | - |
substrate: D-galactose, pH 8.0, temperature not specified in the publication | Haloferax volcanii |
1.1.1.376 | 376 | - |
substrate: L-arabinose, pH 8.0, temperature not specified in the publication | Haloferax volcanii |
2.7.1.58 | 0.148 | - |
purified recombinant enzyme, pH 8.0, 42°C | Haloferax volcanii |
2.7.1.58 | 148 | - |
substrate: 2-dehydro-3-deoxy-D-galactonate, pH and temperature not specified in the publication | Haloferax volcanii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.376 | D-galactose + NAD+ + H2O | the catalytic efficiency for NAD+ is 230 times lower as for NADP+ indicating NADP+ to be the physiological electron acceptor | Haloferax volcanii | D-galactonate + NADH + H+ | - |
? | |
1.1.1.376 | D-galactose + NAD+ + H2O | the catalytic efficiency for NAD+ is 230 times lower as for NADP+ indicating NADP+ to be the physiological electron acceptor | Haloferax volcanii ATCC 29605 | D-galactonate + NADH + H+ | - |
? | |
1.1.1.376 | D-galactose + NADP+ | the enzyme has an essential function during growth on D-galactose | Haloferax volcanii | D-galactono-1,4-lactone + NADPH + H+ | - |
? | |
1.1.1.376 | D-galactose + NADP+ | the enzyme has an essential function during growth on D-galactose | Haloferax volcanii ATCC 29605 | D-galactono-1,4-lactone + NADPH + H+ | - |
? | |
1.1.1.376 | D-galactose + NADP+ + H2O | the catalytic efficiency for NAD+ is 230 times lower as for NADP+ indicating NADP+ to be the physiological electron acceptor | Haloferax volcanii | D-galactonate + NADPH + H+ | - |
? | |
1.1.1.376 | D-galactose + NADP+ + H2O | the catalytic efficiency for NAD+ is 230 times lower as for NADP+ indicating NADP+ to be the physiological electron acceptor | Haloferax volcanii ATCC 29605 | D-galactonate + NADPH + H+ | - |
? | |
1.1.1.376 | L-arabinose + NADP+ + H2O | - |
Haloferax volcanii | L-arabinonate + NADPH + H+ | - |
? | |
1.1.1.376 | L-arabinose + NADP+ + H2O | - |
Haloferax volcanii ATCC 29605 | L-arabinonate + NADPH + H+ | - |
? | |
1.1.1.376 | additional information | low activity was observed with D-xylose (5%), D-glucose, D-fructose and D-mannose are not oxidized at significant rates | Haloferax volcanii | ? | - |
- |
|
1.1.1.376 | additional information | low activity was observed with D-xylose (5%), D-glucose, D-fructose and D-mannose are not oxidized at significant rates | Haloferax volcanii ATCC 29605 | ? | - |
- |
|
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-galactonate | - |
Haloferax volcanii | ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-galactonate | - |
Haloferax volcanii NCIMB 2012 | ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-galactonate | - |
Haloferax volcanii JCM 8879 | ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-galactonate | - |
Haloferax volcanii H26 | ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-galactonate | - |
Haloferax volcanii DS2 | ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-galactonate | - |
Haloferax volcanii DSM 3757 | ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-galactonate | - |
Haloferax volcanii ATCC 29605 | ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-galactonate | - |
Haloferax volcanii NBRC 14742 | ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-galactonate | - |
Haloferax volcanii VKM B-1768 | ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-gluconate | - |
Haloferax volcanii | ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-gluconate | - |
Haloferax volcanii NCIMB 2012 | ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-gluconate | - |
Haloferax volcanii JCM 8879 | ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-gluconate | - |
Haloferax volcanii H26 | ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-gluconate | - |
Haloferax volcanii DS2 | ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-gluconate | - |
Haloferax volcanii DSM 3757 | ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-gluconate | - |
Haloferax volcanii ATCC 29605 | ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-gluconate | - |
Haloferax volcanii NBRC 14742 | ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate | - |
? | |
2.7.1.58 | ATP + 2-dehydro-3-deoxy-D-gluconate | - |
Haloferax volcanii VKM B-1768 | ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.376 | homodimer | 2 * 39000, calculated from sequence | Haloferax volcanii |
2.7.1.58 | hexamer | 6 * 34000, calculated from sequence | Haloferax volcanii |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.376 | HVO_A0330 | - |
Haloferax volcanii |
2.7.1.58 | 2-keto-3-deoxygalactonate kinase | - |
Haloferax volcanii |
2.7.1.58 | HVO A0328 | - |
Haloferax volcanii |
2.7.1.58 | HVO_A0328 | - |
Haloferax volcanii |
2.7.1.58 | KDGal kinase | - |
Haloferax volcanii |
2.7.1.58 | KDGK2 | UniProt | Haloferax volcanii |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.1.58 | 42 | - |
assay at | Haloferax volcanii |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.376 | 8 | - |
- |
Haloferax volcanii |
2.7.1.58 | 8 | - |
assay at | Haloferax volcanii |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.376 | NAD+ | the catalytic efficiency for NAD+ is 230 times lower as for NADP+ indicating NADP+ to be the physiological electron acceptor | Haloferax volcanii | |
1.1.1.376 | NADP+ | the catalytic efficiency for NAD+ is 230 times lower as for NADP+ indicating NADP+ to be the physiological electron acceptor | Haloferax volcanii |
EC Number | Organism | Comment | Expression |
---|---|---|---|
2.7.1.58 | Haloferax volcanii | transcriptional regulator GacR is an activator of genes of the DeLey-Doudoroff pathway including the gene that encodes 2-keto-3-deoxygalactonate kinase | up |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.1.1.376 | malfunction | the deletion mutant does not grow on D-galactose | Haloferax volcanii |
1.1.1.376 | metabolism | the enzyme is part of the De Ley-Doudoroff pathway | Haloferax volcanii |
2.7.1.58 | malfunction | growth studies with knock-out mutants indicate the functional involvement of galactose dehydrogenase, galactonate dehydratase, and KDPGal aldolase in D-galactose degradation | Haloferax volcanii |
2.7.1.58 | malfunction | the deletion mutant does not grow on D-galactose | Haloferax volcanii |
2.7.1.58 | 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 | Haloferax volcanii |
2.7.1.58 | metabolism | the enzyme is part of the De Ley-Doudoroff pathway | Haloferax volcanii |
2.7.1.58 | physiological function | the enzyme is required for D-galactose degradation via the DeLey-Doudoroff pathway in the domain of archaea | Haloferax volcanii |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.376 | 7 | - |
L-arabinose | pH 8.0, temperature not specified in the publication | Haloferax volcanii | |
1.1.1.376 | 9.1 | - |
D-galactose | pH 8.0, temperature not specified in the publication | Haloferax volcanii | |
2.7.1.58 | 8 | - |
2-dehydro-3-deoxy-D-gluconate | pH and temperature not specified in the publication | Haloferax volcanii | |
2.7.1.58 | 432 | - |
2-dehydro-3-deoxy-D-galactonate | pH and temperature not specified in the publication | Haloferax volcanii |