UniProt functional annotation for K5BDL0



	UniProt functional annotation for K5BDL0

UniProt code: K5BDL0.

Organism: Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849) (Mycobacterium hassiacum).

Taxonomy: Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycolicibacterium.

Function: Catalyzes the hydrolysis of glucosylglycerate (GG) to glycerate and glucose (PubMed:25341489, PubMed:31316802). Involved in recovery from nitrogen starvation by promoting the rapid mobilization of the glucosylglycerate that accumulates under these conditions (PubMed:25341489). Can also hydrolyze mannosylglycerate (MG), with tenfold lower efficiency (PubMed:31316802). {ECO:0000269|PubMed:25341489, ECO:0000269|PubMed:31316802}.

Catalytic activity: Reaction=(2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + H2O = (R)- glycerate + D-glucose; Xref=Rhea:RHEA:32059, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:16659, ChEBI:CHEBI:62510; EC=3.2.1.208; Evidence={ECO:0000269|PubMed:25341489, ECO:0000269|PubMed:31316802};

Activity regulation: Activity is not dependent on divalent cations, but it is enhanced by Mg(2+). {ECO:0000269|PubMed:25341489}.

Biophysicochemical properties: Kinetic parameters: KM=16.7 mM for glucosylglycerate (at 37 degrees Celsius, C-terminally tagged variant) {ECO:0000269|PubMed:25341489}; KM=16.7 mM for glucosylglycerate (at 42 degrees Celsius, C-terminally tagged variant) {ECO:0000269|PubMed:25341489}; KM=11.2 mM for glucosylglycerate (at 50 degrees Celsius, C-terminally tagged variant) {ECO:0000269|PubMed:25341489}; Vmax=13.7 umol/min/mg enzyme with glucosylglycerate as substrate (at 37 degrees Celsius, C-terminally tagged variant) {ECO:0000269|PubMed:25341489}; Vmax=15.2 umol/min/mg enzyme with glucosylglycerate as substrate (at 42 degrees Celsius, C-terminally tagged variant) {ECO:0000269|PubMed:25341489}; Vmax=12.3 umol/min/mg enzyme with glucosylglycerate as substrate (at 50 degrees Celsius, C-terminally tagged variant) {ECO:0000269|PubMed:25341489}; Vmax=3.60 umol/min/mg enzyme with glucosylglycerate as substrate (at 50 degrees Celsius, tag-less variant) {ECO:0000269|PubMed:31316802}; Vmax=3.09 umol/min/mg enzyme with mannosylglycerate as substrate (at 50 degrees Celsius, tag-less variant) {ECO:0000269|PubMed:31316802}; pH dependence: Optimum pH is 6.0 (tag-less variant) (PubMed:31316802). Optimum pH is 5.8 (C-terminally tagged variant) (PubMed:25341489). {ECO:0000269|PubMed:25341489, ECO:0000269|PubMed:31316802}; Temperature dependence: Optimum temperature is 50-55 degrees Celsius (tag-less variant) (PubMed:31316802). Optimum temperature is 42 degrees Celsius (C- terminally tagged variant) (PubMed:25341489). {ECO:0000269|PubMed:25341489, ECO:0000269|PubMed:31316802};

Subunit: Homotetramer. Dimer of dimers. {ECO:0000269|PubMed:28876234, ECO:0000269|PubMed:31316802}.

Induction: Up-regulated in response to nitrogen shock. {ECO:0000269|PubMed:25341489}.

Similarity: Belongs to the glycosyl hydrolase 63 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849) (Mycobacterium hassiacum).
Taxonomy:		Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycolicibacterium.



Function:		Catalyzes the hydrolysis of glucosylglycerate (GG) to glycerate and glucose (PubMed:25341489, PubMed:31316802). Involved in recovery from nitrogen starvation by promoting the rapid mobilization of the glucosylglycerate that accumulates under these conditions (PubMed:25341489). Can also hydrolyze mannosylglycerate (MG), with tenfold lower efficiency (PubMed:31316802). {ECO:0000269\|PubMed:25341489, ECO:0000269\|PubMed:31316802}.


Catalytic activity:		Reaction=(2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + H2O = (R)- glycerate + D-glucose; Xref=Rhea:RHEA:32059, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:16659, ChEBI:CHEBI:62510; EC=3.2.1.208; Evidence={ECO:0000269\|PubMed:25341489, ECO:0000269\|PubMed:31316802};
Activity regulation:		Activity is not dependent on divalent cations, but it is enhanced by Mg(2+). {ECO:0000269\|PubMed:25341489}.
Biophysicochemical properties:		Kinetic parameters: KM=16.7 mM for glucosylglycerate (at 37 degrees Celsius, C-terminally tagged variant) {ECO:0000269\|PubMed:25341489}; KM=16.7 mM for glucosylglycerate (at 42 degrees Celsius, C-terminally tagged variant) {ECO:0000269\|PubMed:25341489}; KM=11.2 mM for glucosylglycerate (at 50 degrees Celsius, C-terminally tagged variant) {ECO:0000269\|PubMed:25341489}; Vmax=13.7 umol/min/mg enzyme with glucosylglycerate as substrate (at 37 degrees Celsius, C-terminally tagged variant) {ECO:0000269\|PubMed:25341489}; Vmax=15.2 umol/min/mg enzyme with glucosylglycerate as substrate (at 42 degrees Celsius, C-terminally tagged variant) {ECO:0000269\|PubMed:25341489}; Vmax=12.3 umol/min/mg enzyme with glucosylglycerate as substrate (at 50 degrees Celsius, C-terminally tagged variant) {ECO:0000269\|PubMed:25341489}; Vmax=3.60 umol/min/mg enzyme with glucosylglycerate as substrate (at 50 degrees Celsius, tag-less variant) {ECO:0000269\|PubMed:31316802}; Vmax=3.09 umol/min/mg enzyme with mannosylglycerate as substrate (at 50 degrees Celsius, tag-less variant) {ECO:0000269\|PubMed:31316802}; pH dependence: Optimum pH is 6.0 (tag-less variant) (PubMed:31316802). Optimum pH is 5.8 (C-terminally tagged variant) (PubMed:25341489). {ECO:0000269\|PubMed:25341489, ECO:0000269\|PubMed:31316802}; Temperature dependence: Optimum temperature is 50-55 degrees Celsius (tag-less variant) (PubMed:31316802). Optimum temperature is 42 degrees Celsius (C- terminally tagged variant) (PubMed:25341489). {ECO:0000269\|PubMed:25341489, ECO:0000269\|PubMed:31316802};
Subunit:		Homotetramer. Dimer of dimers. {ECO:0000269\|PubMed:28876234, ECO:0000269\|PubMed:31316802}.
Induction:		Up-regulated in response to nitrogen shock. {ECO:0000269\|PubMed:25341489}.
Similarity:		Belongs to the glycosyl hydrolase 63 family. {ECO:0000305}.