IED ID | IndEnz0001000820 |
Enzyme Type ID | amylase000820 |
Protein Name |
Glucosylglycerol phosphorylase GGoP EC 2.4.1.359 2-O-alpha-D-glucopyranosylglycerol:phosphate alpha-D-glucosyltransferase 2-O-alpha-D-glucosylglycerol phosphorylase retaining |
Gene Name | gtfA HP15_2853 |
Organism | Marinobacter adhaerens (strain DSM 23420 / HP15) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Marinobacteraceae Marinobacter Marinobacter adhaerens Marinobacter adhaerens (strain DSM 23420 / HP15) |
Enzyme Sequence | MLLKNAVQLICYPDRIGNNLKDLYTVVDTHLSEAIGGLHILPFFPSNADGGFSPLTHKEVDPKVGTWDDIEAFTAKYDLCVDLTVNHISDESPEFTDFIANGFDSEYADLFVHVDKFGEISPDDMAKIHIRKEKEPFREVTLSDGTKTRVWCTFTEQQIDLNYESDLAYQLMESYIGFLTSKGVNLLRLDAFGYTTKRIGTSCFLVEPEVYQILDWVNQVALKHGAECLPEVHDHTSYQYAISRRNMHPYGFALPPLLLYSLLDANSTYLKNWLRMCPRNMVTVLDTHDGICIPDVEGVLPDEKIKVLIDNIDARSADPIMRRSAANIHSVGAIYQLTCTFYDALMQNDDAYIAARAIQFFTPGIPQVYYVGLLAGCNDHELMEQSGELRDINRHYYTLEEVEQDIQKPVVQRLLSLMKFRSNYPAFDGHFELNYSNNSSVAMAWRHGDYYCHLFVDLNFKTVKVTYTDVETGETRHLEC |
Enzyme Length | 480 |
Uniprot Accession Number | E4PMA5 |
Absorption | |
Active Site | ACT_SITE 190; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:A0ZZH6; ACT_SITE 231; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:A0ZZH6 |
Activity Regulation | |
Binding Site | BINDING 194; /note=Substrate; /evidence=ECO:0000305|PubMed:29470619; BINDING 336; /note=Substrate; /evidence=ECO:0000305|PubMed:29470619 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=2-O-(alpha-D-glucopyranosyl)glycerol + phosphate = alpha-D-glucose 1-phosphate + glycerol; Xref=Rhea:RHEA:56416, ChEBI:CHEBI:17754, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601, ChEBI:CHEBI:82766; EC=2.4.1.359; Evidence={ECO:0000269|PubMed:29470619}; |
DNA Binding | |
EC Number | 2.4.1.359 |
Enzyme Function | FUNCTION: Catalyzes the reversible phosphorolysis of 2-O-alpha-D-glucosylglycerol with retention of the anomeric configuration, forming alpha-D-glucose 1-phosphate and glycerol. Has most likely a catabolic role, either regulating the intracellular levels of glucosylglycerol, which acts as a compatible solute, or degrading it when the environmental conditions change. Cannot catalyze the phosphorolysis of sucrose or glucosylglycerate. {ECO:0000269|PubMed:29470619}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. Full activity is retained after incubating at up to 45 degrees Celsius for 10 minutes, while only 46% is left after incubating at 50 degrees Celsius. The protein is completely denatured after incubating at higher temperatures. {ECO:0000269|PubMed:29470619}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:29470619}; |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Binding site (2); Chain (1); Mutagenesis (3) |
Keywords | Carbohydrate metabolism;Glycosyltransferase;Transferase |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 54,825 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.9 mM for 2-O-(alpha-D-glucopyranosyl)glycerol (at pH 6.5 and 37 degrees Celsius) {ECO:0000269|PubMed:29470619}; KM=10 mM for phosphate (at pH 6.5 and 37 degrees Celsius) {ECO:0000269|PubMed:29470619}; KM=2.5 mM for alpha-D-glucose 1-phosphate (at pH 6.5 and 37 degrees Celsius) {ECO:0000269|PubMed:29470619}; KM=7.0 mM for glycerol (at pH 6.5 and 37 degrees Celsius) {ECO:0000269|PubMed:29470619}; Note=kcat is 14 sec(-1) towards 2-O-(alpha-D-glucopyranosyl)glycerol for the phosphorolytic direction (at pH 6.5 and 37 degrees Celsius). kcat is 14 sec(-1) towards phosphate for the phosphorolytic direction (at pH 6.5 and 37 degrees Celsius). kcat is 36 sec(-1) towards alpha-D-glucose 1-phosphate for the synthetic direction (at pH 6.5 and 37 degrees Celsius). kcat is 39 sec(-1) towards glycerol for the synthetic direction (at pH 6.5 and 37 degrees Celsius). {ECO:0000269|PubMed:29470619}; |
Metal Binding | |
Rhea ID | RHEA:56416 |
Cross Reference Brenda | 2.4.1.359; |