Q9SM60 · PGMC_PEA
- ProteinPhosphoglucomutase, cytoplasmic
- GenePGM1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids582 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Catalyzes the reversible isomerization of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate (By similarity).
The mechanism proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate (By similarity).
This enzyme participates in both the breakdown and synthesis of glucose (By similarity).
The mechanism proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate (By similarity).
This enzyme participates in both the breakdown and synthesis of glucose (By similarity).
Catalytic activity
- alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate
- alpha-D-glucose 1-phosphate + O-phospho-L-seryl-[protein] = alpha-D-glucose 1,6-bisphosphate + L-seryl-[protein]
- alpha-D-glucose 1,6-bisphosphate + L-seryl-[protein] = alpha-D-glucose 6-phosphate + O-phospho-L-seryl-[protein]
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 25 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 124 | Phosphoserine intermediate | ||||
Sequence: S | ||||||
Binding site | 124 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 124 | Mg2+ (UniProtKB | ChEBI); via phosphate group | ||||
Sequence: S | ||||||
Binding site | 300 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 302 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 304 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 304 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 305 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 368 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 387 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 389 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 400 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphoglucomutase activity | |
Biological Process | glucose metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphoglucomutase, cytoplasmic
- EC number
- Short namesPGM
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > Hologalegina > IRL clade > Fabeae > Pisum
Accessions
- Primary accessionQ9SM60
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000147804 | 1-582 | Phosphoglucomutase, cytoplasmic | |||
Sequence: MALFTVSRIQTTPFDGQKPGTSGLRKKVKVFVQPHYLENFVQASFNALTEGKVRGATLVVSGDGRYYSEQAIQIITKMAAANGVRRIWIGQNGLLSTPAVSAVIRERVGVDGSKATGSFILTASHNPGGPNEDFGIKYNMENGGPAPEGITNKIYENTTTIKEYLIAPDLPNVDITTVGVTNFTGPEGPFDIEVFDSASDYIKLMKSIFDFESIRKLLTSPKFSFCYDALHGVAGAYAKRIFVDELGAQENSLINCVPKEDFGGGHPDPNLTYAKELVARMGLGKSEPEGEVPEFGAAADGDADRNMVLGKRFFVTPSDSVAIIAANAVEAIPYFSAGLKGVARSMPTSAALDVVAKHLNLKFFEVPTGWKFFGNLMDAGLCSVCGEESFGTGSDHIREKDGIWAVLAWLSILAYKTKDNLESKLVSVEDIVRQHWATYGRHYYTRYDYENVDAGAAKELMAHLVKLQSSLPEVNEIIKGASSDVSKVVHGDEFEYNDPVDGSISSHQGIRYLFEDGSRLIFRLSGTGSEGATIRLYIEQYEKDPSKIGRLSHEALAPLVEAALKLSKMEEFTGRSAPTVIT | ||||||
Modified residue | 124 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Interaction
Subunit
Monomer.
Structure
Sequence
- Sequence statusComplete
- Length582
- Mass (Da)63,325
- Last updated2000-05-01 v1
- Checksum5FF85499D031E2EB