| IED ID | IndEnz0001000668 |
| Enzyme Type ID | amylase000668 |
| Protein Name |
Glucosylglycerate phosphorylase GGa phosphorylase GGaP EC 2.4.1.352 |
| Gene Name | ycjM ggaP b1309 JW1302 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MKQKITDYLDEIYGGTFTATHLQKLVTRLESAKRLITQRRKKHWDESDVVLITYADQFHSNDLKPLPTFNQFYHQWLQSIFSHVHLLPFYPWSSDDGFSVIDYHQVASEAGEWQDIQQLGECSHLMFDFVCNHMSAKSEWFKNYLQQHPGFEDFFIAVDPQTDLSAVTRPRALPLLTPFQMRDHSTRHLWTTFSDDQIDLNYRSPEVLLAMVDVLLCYLAKGAEYVRLDAVGFMWKEPGTSCIHLEKTHLIIKLLRSIIDNVAPGTVIITETNVPHKDNIAYFGAGDDEAHMVYQFSLPPLVLHAVQKQNVEALCAWAQNLTLPSSNTTWFNFLASHDGIGLNPLRGLLPESEILELVEALQQEGALVNWKNNPDGTRSPYEINVTYMDALSRRESSDEERCARFILAHAILLSFPGVPAIYIQSILGSRNDYAGVEKLGYNRAINRKKYHSKEITRELNDEATLRHAVYHELSRLITLRRSHNEFHPDNNFTIDTINSSVMRIPRSNADGNCLTGLFNVSKNIQHVNITNLHGRDLISEVDILGNEITLRPWQVMWIK |
| Enzyme Length | 559 |
| Uniprot Accession Number | P76041 |
| Absorption | |
| Active Site | ACT_SITE 229; /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, ECO:0000269|PubMed:29684280}; |
| 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 (also called (R)-glycerate) (PubMed:28754708, PubMed:29684280). May be a regulator of intracellular levels of glucosylglycerate, a compatible solute that primarily protects organisms facing salt stress and very specific nutritional constraints (PubMed:28754708). Cannot catalyze the phosphorolysis of sucrose (PubMed:28754708). Does not act on other sugars such as alpha-D-galactose 1-phosphate, alpha-D-mannose 1-phosphate or beta-D-glucose 1-phosphate; in vitro D-erythronate can substitute for D-glycerate with a much lower efficiency (PubMed:29684280). {ECO:0000269|PubMed:28754708, ECO:0000269|PubMed:29684280}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1) |
| 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 | 16606699; |
| Motif | |
| Gene Encoded By | |
| Mass | 64,186 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.4 mM for D-glycerate (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:28754708}; KM=69 uM for 2-O-(alpha-D-glucopyranosyl)-D-glycerate (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:29684280}; KM=2.2 mM for phosphate (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:29684280}; KM=9.4 mM for alpha-D-glucose 1-phosphate (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:29684280}; KM=4.4 mM for D-glycerate (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:29684280}; Note=kcat is 2.2 sec(-1) for phosphorolysis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate, kcat is 325 sec(-1) for glyceration of alpha-D-glucose 1-phosphate. {ECO:0000269|PubMed:29684280}; |
| Metal Binding | |
| Rhea ID | RHEA:55268 |
| Cross Reference Brenda |