UniProt functional annotation for P71447

UniProt code: P71447.

Organism: Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
Taxonomy: Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Lactococcus.
 
Function: Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6- (bis)phosphate (beta-G16P) as an intermediate. The beta- phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P. Glucose or lactose are used in preference to maltose, which is only utilized after glucose or lactose has been exhausted. It plays a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose. {ECO:0000269|PubMed:15005616, ECO:0000269|PubMed:9084169}.
 
Catalytic activity: Reaction=beta-D-glucose 1-phosphate = beta-D-glucose 6-phosphate; Xref=Rhea:RHEA:20113, ChEBI:CHEBI:57684, ChEBI:CHEBI:58247; EC=5.4.2.6;
Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:8071206}; Note=Binds 2 magnesium ions per subunit. {ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:8071206};
Activity regulation: Competitively inhibited by alpha-D-galactose-1- phosphate. {ECO:0000269|PubMed:15826149}.
Biophysicochemical properties: Kinetic parameters: KM=14.6 uM for beta-glucose 1-phosphate (at pH 7 and 25 degrees Celsius) {ECO:0000269|PubMed:15005616, ECO:0000269|PubMed:15996095}; KM=20 uM for alpha-D-glucose 1,6-bisphosphate (at pH 7 and 25 degrees Celsius) {ECO:0000269|PubMed:15005616, ECO:0000269|PubMed:15996095}; KM=100 uM for alpha-D-fructose 1,6-bisphosphate (at pH 7 and 25 degrees Celsius) {ECO:0000269|PubMed:15005616, ECO:0000269|PubMed:15996095}; KM=270 uM for magnesium (at pH 7 and 25 degrees Celsius) {ECO:0000269|PubMed:15005616, ECO:0000269|PubMed:15996095}; KM=800 uM for acetyl-phosphate (at pH 7 and 25 degrees Celsius) {ECO:0000269|PubMed:15005616, ECO:0000269|PubMed:15996095}; pH dependence: Optimum pH is around 7. Relatively stable in solution within the pH range of 5-9.5. {ECO:0000269|PubMed:15005616, ECO:0000269|PubMed:15996095};
Subunit: Monomer. {ECO:0000269|PubMed:12081483, ECO:0000269|PubMed:12637673, ECO:0000269|PubMed:15826149, ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:19154134, ECO:0000269|PubMed:20164409, ECO:0000269|PubMed:8071206, ECO:0000269|Ref.10}.
Subcellular location: Cytoplasm {ECO:0000305}.
Induction: By maltose, trehalose and sucrose and repressed by glucose and lactose. {ECO:0000269|PubMed:15005616, ECO:0000269|PubMed:8071206, ECO:0000269|PubMed:9084169}.
Ptm: Autophosphorylated. {ECO:0000269|PubMed:15996095}.
Miscellaneous: The catalysis proceeds via a phosphoenzyme formed by reaction of an active-site nucleophile with the cofactor glucose 1,6- diphosphate (G1,6-diP). The phosphorylated mutase binds either G1P or G6P and transfers the phosphoryl group to the C(6)OH or C(1)OH, respectively.
Similarity: Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.