| IED ID | IndEnz0001000671 |
| Enzyme Type ID | amylase000671 |
| Protein Name |
Glucosylglycerate phosphorylase GGa phosphorylase GGaP EC 2.4.1.352 |
| Gene Name | Mesil_0665 |
| Organism | Meiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) (Thermus silvanus) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Deinococcus-Thermus Deinococci Thermales Thermaceae Meiothermus Meiothermus silvanus Meiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) (Thermus silvanus) |
| Enzyme Sequence | MSSLTPELRQSILEHLGFLYGERAPAVLGRLEEICSGFPAQRREGGWSEKDALLITYGDQIHAEGEPPLQTLYDFLYERLRGVFSGVHLLPFYPSTSDDGFSVVDFQRVDPELGTWTDIRIIAQDFRLMADLVCNHVSASSPWFQGFLQDDPQYQGFFITVDPGTDLSTVFRPRALPLLTPFQTPSGEKLVWTTFSPDQTDLNYANPEVLLEVIEALLCYVRNGAGLIRLDAVGFIWKEIGTSCMHLEGAHRIVKLMRLVLDAVAPHVLLVSETNAPHRENISYFGNGHDEAQLVYQFPLPPLVMHTFRTGDASKLAGWAAGLTLPSERTTFFNFLASHDGIGVVPAGGILQPEEIAALVRQALEHGGRVNHKDTPDGPVPYELCLTLFDALSNPNSDEAEDLKIARFLAANVILLSLQGIPGVYIHSLFGSPSDHAGFEESGIPRRLNRHKFTKAELEERLADPASRAAKILAAYSHLLRVRSMHPAFHPNAPQRILPSTEVLRIVRGEGDQAVGCYINVTDRPQVVSRIGKNLITGQWFTGVLKPYQAAWIID |
| Enzyme Length | 555 |
| Uniprot Accession Number | D7BAR0 |
| Absorption | |
| Active Site | ACT_SITE 231; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:A0ZZH6 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=(2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + phosphate = (R)-glycerate + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:55268, ChEBI:CHEBI:16659, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601, ChEBI:CHEBI:62510; EC=2.4.1.352; Evidence={ECO:0000269|PubMed:28754708}; |
| DNA Binding | |
| EC Number | 2.4.1.352 |
| Enzyme Function | FUNCTION: Catalyzes the reversible phosphorolysis of glucosylglycerate into alpha-D-glucose 1-phosphate (Glc1P) and D-glycerate. May be a regulator of intracellular levels of glucosylglycerate, a compatible solute that primarily protects organisms facing salt stress and very specific nutritional constraints. Has a very strict substrate specificity. Cannot catalyze the phosphorolysis of sucrose or synthesize sucrose from Glc1P and D-fructose. {ECO:0000269|PubMed:28754708}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 42 degrees Celsius. Retains full activity after incubating at up to 55 degrees Celsius for 10 minutes, but only 35% is left after incubating at 60 degrees Celsius. {ECO:0000269|PubMed:28754708}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6 and 6.5 in phosphorolytic and synthetic directions, respectively. {ECO:0000269|PubMed:28754708}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Mutagenesis (3) |
| Keywords | Carbohydrate metabolism;Glycosyltransferase;Reference proteome;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 | 61,531 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.5 mM for 2-O-(alpha-D-glucopyranosyl)-D-glycerate (at pH 6.0 and 42 degrees Celsius) {ECO:0000269|PubMed:28754708}; KM=2.5 mM for phosphate (at pH 6.0 and 42 degrees Celsius) {ECO:0000269|PubMed:28754708}; KM=8.1 mM for alpha-D-glucose 1-phosphate (at pH 6.5 and 42 degrees Celsius) {ECO:0000269|PubMed:28754708}; KM=2.6 mM for D-glycerate (at pH 6.5 and 42 degrees Celsius) {ECO:0000269|PubMed:28754708}; Note=kcat is 0.83 sec(-1) towards 2-O-(alpha-D-glucopyranosyl)-D-glycerate for the phosphorolytic direction (at pH 6.0 and 42 degrees Celsius). kcat is 0.98 sec(-1) towards phosphate for the phosphorolytic direction (at pH 6.0 and 42 degrees Celsius). kcat is 96 sec(-1) towards alpha-D-glucose 1-phosphate for the synthetic direction (at pH 6.5 and 42 degrees Celsius). kcat is 128 sec(-1) towards D-glycerate for the synthetic direction (at pH 6.5 and 42 degrees Celsius). {ECO:0000269|PubMed:28754708}; |
| Metal Binding | |
| Rhea ID | RHEA:55268 |
| Cross Reference Brenda | 2.4.1.352; |