Detail Information for IndEnz0001000820
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;