P37012 · PGM2_YEAST
- ProteinPhosphoglucomutase 2
- GenePGM2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids569 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Major phosphoglucomutase isozyme that catalyzes the reversible isomerization of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate (PubMed:1100398, PubMed:23103740, PubMed:4992300, PubMed:5784209).
The mechanism proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate (Probable). Constitutes about 80-90% of the phosphoglucomutase activity in the cell (PubMed:14264884, PubMed:5231755).
Key enzyme in hexose metabolism. The forward reaction is an essential step in the energy metabolism of galactose since the product of the galactose pathway enzymes in yeast is glucose 1-phosphate. The reverse reaction is an essential step for biosynthesis when carbon sources other than galactose are the energy source because glucose 1-phosphate is the starting point for the synthesis of UDP-glucose, which acts as a precursor for the synthesis of oligosaccharides and trehalose (PubMed:14264884).
The mechanism proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate (Probable). Constitutes about 80-90% of the phosphoglucomutase activity in the cell (PubMed:14264884, PubMed:5231755).
Key enzyme in hexose metabolism. The forward reaction is an essential step in the energy metabolism of galactose since the product of the galactose pathway enzymes in yeast is glucose 1-phosphate. The reverse reaction is an essential step for biosynthesis when carbon sources other than galactose are the energy source because glucose 1-phosphate is the starting point for the synthesis of UDP-glucose, which acts as a precursor for the synthesis of oligosaccharides and trehalose (PubMed:14264884).
Miscellaneous
Present with 3790 molecules/cell in log phase SD medium.
Catalytic activity
- alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate
- O-phospho-L-seryl-[protein] + alpha-D-glucose 1-phosphate = alpha-D-glucose 1,6-bisphosphate + L-seryl-[protein]
- alpha-D-glucose 1,6-bisphosphate + L-seryl-[protein] = O-phospho-L-seryl-[protein] + alpha-D-glucose 6-phosphate
Cofactor
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )
Note: Binds 1 magnesium ion per subunit. Can also use Zn2+ as cofactor.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
2.24 μM | alpha-D-glucose 1,6-diphosphate | |||||
23.4 μM | alpha-D-glucose 1-phosphate | |||||
26 μM | alpha-D-glucose 1-phosphate | |||||
530 μM | D-ribose 1-phosphate |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
33.7 μmol/min/mg | for alpha-D-glucose 1-phosphate | ||||
0.32 μmol/min/mg | for D-ribose 1-phosphate |
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 24 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | |||
Active site | 119 | Phosphoserine intermediate | |||
Binding site | 119 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | |||
Binding site | 119 | Mg2+ (UniProtKB | ChEBI); via phosphate group | |||
Binding site | 290 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 292 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 294 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | |||
Binding site | 294 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 295 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | |||
Binding site | 359 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | |||
Binding site | 378 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | |||
Binding site | 380 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | |||
Binding site | 391 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphoglucomutase activity | |
Biological Process | carbohydrate metabolic process | |
Biological Process | galactose catabolic process | |
Biological Process | glucose 1-phosphate metabolic process | |
Biological Process | glucose 6-phosphate metabolic process | |
Biological Process | glucose metabolic process | |
Biological Process | glycogen biosynthetic process | |
Biological Process | intracellular calcium ion homeostasis | |
Biological Process | intracellular monoatomic cation homeostasis | |
Biological Process | trehalose biosynthetic process | |
Biological Process | UDP-glucose metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphoglucomutase 2
- EC number
- Short namesPGM 2
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP37012
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Blocks galactose utilization, but does not impair growth on glucose.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 5 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Initiator methionine | 1 | Removed | |||
Modified residue | 2 | N-acetylserine | |||
Chain | PRO_0000147797 | 2-569 | Phosphoglucomutase 2 | ||
Modified residue | 111 | Phosphothreonine | |||
Modified residue | 117 | Phosphothreonine | |||
Modified residue | 119 | Phosphoserine | |||
Post-translational modification
O-glycosylated with mannose residues (By similarity).
Substrate of UDP-glucose--glycoprotein glucose phosphotransferase, linking glucose in a phosphodiester linkage to O-linked mannose (PubMed:7929458, PubMed:8385141).
Substrate of UDP-glucose--glycoprotein glucose phosphotransferase, linking glucose in a phosphodiester linkage to O-linked mannose (PubMed:7929458, PubMed:8385141).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Induced in response to galactose and severely repressed in response to glucose.
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length569
- Mass (Da)63,089
- Last updated1994-06-01 v1
- Checksum45B78AFF8197645E
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Sequence conflict | 27 | in Ref. 6; AA sequence | |||
Sequence conflict | 32 | in Ref. 6; AA sequence | |||
Sequence conflict | 272 | in Ref. 6; AA sequence | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X74823 EMBL· GenBank· DDBJ | CAA52820.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U09499 EMBL· GenBank· DDBJ | AAA91282.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z49702 EMBL· GenBank· DDBJ | CAA89741.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY723853 EMBL· GenBank· DDBJ | AAU09770.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006946 EMBL· GenBank· DDBJ | DAA10001.1 EMBL· GenBank· DDBJ | Genomic DNA |