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UniProt functional annotation for O93715 | ||
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| UniProt code: O93715. |
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| Organism: | |
Saccharolobus solfataricus (Sulfolobus solfataricus). |
| Taxonomy: | |
Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; Saccharolobus. |
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| Function: | |
Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Displays broad substrate specificity since it is able to catalyze the oxidation of a number of alternative aldose sugars, such as D-galactose, D-xylose and L-arabinose, to the corresponding glyconate. Can utilize both NAD(+) and NADP(+) as electron acceptor. Physiologically, seems to be involved in the degradation of both glucose and galactose through a non-phosphorylative variant of the Entner-Doudoroff pathway. {ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812}. |
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| Catalytic activity: | |
Reaction=D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH; Xref=Rhea:RHEA:14293, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:16217, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.47; Evidence={ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812}; |
| Catalytic activity: | |
Reaction=D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH; Xref=Rhea:RHEA:14293, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:16217, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.359; Evidence={ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812}; |
| Catalytic activity: | |
Reaction=D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:14405, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:16217, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.47; Evidence={ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812}; |
| Catalytic activity: | |
Reaction=D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:14405, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:16217, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.359; Evidence={ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812}; |
| Catalytic activity: | |
Reaction=D-galactose + NAD(+) = D-galactono-1,4-lactone + H(+) + NADH; Xref=Rhea:RHEA:21296, ChEBI:CHEBI:4139, ChEBI:CHEBI:15378, ChEBI:CHEBI:15895, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.48; Evidence={ECO:0000269|PubMed:12824170}; |
| Catalytic activity: | |
Reaction=D-galactose + NADP(+) = D-galactono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:18625, ChEBI:CHEBI:4139, ChEBI:CHEBI:15378, ChEBI:CHEBI:15945, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.359; Evidence={ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812}; |
| Catalytic activity: | |
Reaction=D-galactose + NADP(+) = D-galactono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:18625, ChEBI:CHEBI:4139, ChEBI:CHEBI:15378, ChEBI:CHEBI:15945, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.120; Evidence={ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812}; |
| Catalytic activity: | |
Reaction=an aldopyranose + NAD(+) = aldono-1,5-lactone + H(+) + NADH; Xref=Rhea:RHEA:15917, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:140379, ChEBI:CHEBI:140380; EC=1.1.1.359; Evidence={ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812}; |
| Catalytic activity: | |
Reaction=an aldopyranose + NADP(+) = aldono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:36587, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:140379, ChEBI:CHEBI:140380; EC=1.1.1.359; Evidence={ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:3827812}; |
| Cofactor: | |
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16556607}; Note=Binds 2 Zn(2+) ions per subunit. One of the zinc atoms is essential for catalytic activity while the other has a structural function. {ECO:0000269|PubMed:16556607}; |
| Activity regulation: | |
Inhibited by EDTA in vitro. {ECO:0000269|PubMed:3827812}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=8.0 mM for D-glucose (in the presence of NAD(+), at 70 degrees Celsius and pH 8) {ECO:0000269|PubMed:3827812}; KM=1.50 mM for D-glucose (in the presence of NAD(+), at 70 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12824170}; KM=0.44 mM for D-glucose (in the presence of NADP(+), at 70 degrees Celsius and pH 8) {ECO:0000269|PubMed:3827812}; KM=1.30 mM for D-glucose (in the presence of NADP(+), at 70 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12824170}; KM=0.57 mM for D-galactose (in the presence of NAD(+), at 70 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12824170}; KM=22 mM for D-galactose (in the presence of NADP(+), at 70 degrees Celsius and pH 8) {ECO:0000269|PubMed:3827812}; KM=0.44 mM for D-galactose (in the presence of NADP(+), at 70 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12824170}; KM=0.25 mM for D-xylose (in the presence of NAD(+), at 70 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:16556607}; KM=0.18 mM for D-xylose (in the presence of NADP(+), at 70 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:16556607}; KM=1.2 mM for NAD(+) (at 70 degrees Celsius and pH 8) {ECO:0000269|PubMed:3827812}; KM=0.03 mM for NADP(+) (at 70 degrees Celsius and pH 8) {ECO:0000269|PubMed:3827812}; Vmax=110 umol/min/mg enzyme for the oxidation of D-glucose by NAD(+) (at 70 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12824170}; Vmax=70 umol/min/mg enzyme for the oxidation of D-glucose by NADP(+) (at 70 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12824170}; Vmax=90 umol/min/mg enzyme for the oxidation of D-galactose by NAD(+) (at 70 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12824170}; Vmax=55 umol/min/mg enzyme for the oxidation of D-galactose by NADP(+) (at 70 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:12824170}; Vmax=90 umol/min/mg enzyme for the oxidation of D-xylose by NAD(+) (at 70 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:16556607}; Vmax=65 umol/min/mg enzyme for the oxidation of D-xylose by NADP(+) (at 70 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:16556607}; pH dependence: Optimum pH is 9. {ECO:0000269|PubMed:3827812}; Temperature dependence: Optimum temperature is 77 degrees Celsius. At 37 degrees Celsius, shows about 20% activity as compared with the maximal value. {ECO:0000269|PubMed:3827812}; |
| Subunit: | |
Homotetramer. {ECO:0000269|PubMed:12824170, ECO:0000269|PubMed:16556607, ECO:0000269|PubMed:3827812}. |
| Similarity: | |
Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily. {ECO:0000255|HAMAP- Rule:MF_02127}. |
Annotations taken from UniProtKB at the EBI.