P37012 · PGM2_YEAST

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).

Miscellaneous

Present with 3790 molecules/cell in log phase SD medium.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

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 μMalpha-D-glucose 1,6-diphosphate
23.4 μMalpha-D-glucose 1-phosphate
26 μMalpha-D-glucose 1-phosphate
530 μMD-ribose 1-phosphate
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
33.7 μmol/min/mgfor alpha-D-glucose 1-phosphate
0.32 μmol/min/mgfor D-ribose 1-phosphate

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site24alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI)
Active site119Phosphoserine intermediate
Binding site119alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI)
Binding site119Mg2+ (UniProtKB | ChEBI); via phosphate group
Binding site290Mg2+ (UniProtKB | ChEBI)
Binding site292Mg2+ (UniProtKB | ChEBI)
Binding site294alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI)
Binding site294Mg2+ (UniProtKB | ChEBI)
Binding site295alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI)
Binding site359alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI)
Binding site378alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI)
Binding site380alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI)
Binding site391alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Molecular Functionmagnesium ion binding
Molecular Functionphosphoglucomutase activity
Biological Processcarbohydrate metabolic process
Biological Processgalactose catabolic process
Biological Processglucose 1-phosphate metabolic process
Biological Processglucose 6-phosphate metabolic process
Biological Processglucose metabolic process
Biological Processglycogen biosynthetic process
Biological Processintracellular calcium ion homeostasis
Biological Processintracellular monoatomic cation homeostasis
Biological Processtrehalose biosynthetic process
Biological ProcessUDP-glucose metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphoglucomutase 2
  • EC number
  • Short names
    PGM 2
  • Alternative names
    • D-glucose-1,6-diphosphate:D-glucose-1-phosphate phosphotransferase
    • Glucose phosphomutase 2

Gene names

    • Name
      PGM2
    • Synonyms
      GA-5
      , GAL5
    • ORF names
      YM9718.04C
    • Ordered locus names
      YMR105C

Organism names

Accessions

  • Primary accession
    P37012
  • Secondary accessions
    • D6VZS7

Proteomes

Organism-specific databases

Subcellular Location

Keywords

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.

Go to variant viewer

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

Type
IDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylserine
ChainPRO_00001477972-569Phosphoglucomutase 2
Modified residue111Phosphothreonine
Modified residue117Phosphothreonine
Modified residue119Phosphoserine

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).

Keywords

Proteomic databases

PTM databases

Expression

Induction

Induced in response to galactose and severely repressed in response to glucose.

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-23Disordered

Sequence similarities

Belongs to the phosphohexose mutase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    569
  • Mass (Da)
    63,089
  • Last updated
    1994-06-01 v1
  • Checksum
    45B78AFF8197645E
MSFQIETVPTKPYEDQKPGTSGLRKKTKVFKDEPNYTENFIQSIMEAIPEGSKGATLVVGGDGRYYNDVILHKIAAIGAANGIKKLVIGQHGLLSTPAASHIMRTYEEKCTGGIILTASHNPGGPENDMGIKYNLSNGGPAPESVTNAIWEISKKLTSYKIIKDFPELDLGTIGKNKKYGPLLVDIIDITKDYVNFLKEIFDFDLIKKFIDNQRSTKNWKLLFDSMNGVTGPYGKAIFVDEFGLPADEVLQNWHPSPDFGGMHPDPNLTYASSLVKRVDREKIEFGAASDGDGDRNMIYGYGPSFVSPGDSVAIIAEYAAEIPYFAKQGIYGLARSFPTSGAIDRVAKAHGLNCYEVPTGWKFFCALFDAKKLSICGEESFGTGSNHVREKDGVWAIMAWLNILAIYNKHHPENEASIKTIQNEFWAKYGRTFFTRYDFEKVETEKANKIVDQLRAYVTKSGVVNSAFPADESLKVTDCGDFSYTDLDGSVSDHQGLYVKLSNGARFVLRLSGTGSSGATIRLYIEKYCDDKSQYQKTAEEYLKPIINSVIKFLNFKQVLGTEEPTVRT

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict27in Ref. 6; AA sequence
Sequence conflict32in Ref. 6; AA sequence
Sequence conflict272in Ref. 6; AA sequence

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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