UniProt functional annotation for Q8ZWV0

UniProt code: Q8ZWV0.

Organism: Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827).
Taxonomy: Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae; Pyrobaculum.
 
Function: Catalyzes the isomerization of both glucose 6-phosphate and epimeric mannose 6-phosphate at a similar catalytic efficiency.
 
Catalytic activity: Reaction=aldehydo-D-glucose 6-phosphate = keto-D-fructose 6-phosphate; Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57579, ChEBI:CHEBI:57584; EC=5.3.1.9;
Catalytic activity: Reaction=D-mannose 6-phosphate = D-fructose 6-phosphate; Xref=Rhea:RHEA:12356, ChEBI:CHEBI:58735, ChEBI:CHEBI:61527; EC=5.3.1.8;
Activity regulation: Inhibited by 5-phosphoarabinonate (PAB) and 6- phosphogluconate.
Biophysicochemical properties: Kinetic parameters: KM=2.7 mM for glucose 6-phosphate (at 50 degrees Celsius) {ECO:0000269|PubMed:15290326}; KM=0.3 mM for fructose 6-phosphate (at 50 degrees Celsius) {ECO:0000269|PubMed:15290326}; KM=1.9 mM for glucose 6-phosphate (at 80 degrees Celsius) {ECO:0000269|PubMed:15290326}; KM=0.06 mM for fructose 6-phosphate (at 80 degrees Celsius) {ECO:0000269|PubMed:15290326}; KM=0.49 mM for mannose 6-phosphate (at 80 degrees Celsius) {ECO:0000269|PubMed:15290326}; Vmax=50 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at 50 degrees Celsius) {ECO:0000269|PubMed:15290326}; Vmax=31.3 mmol/min/mg enzyme with fructose 6-phosphate as substrate (at 50 degrees Celsius) {ECO:0000269|PubMed:15290326}; Vmax=150 mmol/min/mg enzyme with glucose 6-phosphate as substrate (at 80 degrees Celsius) {ECO:0000269|PubMed:15290326}; Vmax=109 mmol/min/mg enzyme with fructose 6-phosphate as substrate (at 80 degrees Celsius) {ECO:0000269|PubMed:15290326}; Vmax=117 mmol/min/mg enzyme with mannose 6-phosphate as substrate (at 80 degrees Celsius) {ECO:0000269|PubMed:15290326}; pH dependence: Optimum pH is 7.4. {ECO:0000269|PubMed:15290326}; Temperature dependence: Optimum temperature is 100 degrees Celsius. {ECO:0000269|PubMed:15290326};
Subunit: Homodimer. {ECO:0000269|PubMed:15252053}.
Miscellaneous: The lack of any movement in response to the binding of ligand may be due to its inherent thermostability, which would tend to restrict any flexibility in the protein.
Similarity: Belongs to the PGI/PMI family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.