Q9SM59 · PGMP_PEA
- ProteinPhosphoglucomutase, chloroplastic
- GenePGMP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids626 (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.
Activity regulation
Inhibited by the Calvin cycle intermediates fructose-1,6-bisphosphate and ribulose-1,5-bisphosphate.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 91 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 184 | Phosphoserine intermediate | ||||
Sequence: S | ||||||
Binding site | 184 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 184 | Mg2+ (UniProtKB | ChEBI); via phosphate group | ||||
Sequence: S | ||||||
Binding site | 349 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 351 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 353 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 353 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 354 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 417 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 436 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 438 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 449 | alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
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, chloroplastic
- 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 accessionQ9SM59
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-66 | Chloroplast | ||||
Sequence: MAFCYRLDNFIISAFKPKHSNVPLSIHHSSSNFPSFKVQNFPFRVRYNSAIRATSSSSSTPTTIAE | ||||||
Chain | PRO_0000023897 | 67-626 | Phosphoglucomutase, chloroplastic | |||
Sequence: PNDIKINSIPTKPIEGQKTGTSGLRKKVKVFKQENYLANWIQALFNSLPPEDYKNGLLVLGGDGRYFNKEAAQIIIKIAAGNGVGKILVGKEGILSTPAVSAVIRKREANGGFIMSASHNPGGPEYDWGIKFNYSSGQPAPESITDKIYGNTLSISEIKIADIPDVDLSNVGVTKFGSFSVEVIDPVSDYLELLETVFDFQLIKSLISRPDFRFTFDAMHAVAGAYATPIFVDKLSASLDSISNGIPLEDFGHGHPDPNLTYAKDLVKIMYAENGPDFGAASDGDGDRNMILGTSFFVTPSDSVAVIAANAKEAIPYFKDSIKGLARSMPTSGALDRVAEKLNLPFFEVPTGWKFFGNLMDAGNLSICGEESFGTGSDHIREKDGIWAVLAWLSIIAHRNKDTKPGEKLVSVSDVVKEHWATYGRNFFSRYDYEECESEGANKMIEYLRELLSKSKPGDKYGSYVLQFADDFTYTDPVDGSVVSKQGVRFVFTDGSRIIYRLSGTGSAGATVRVYIEQFEPDVSKHDVDAQIALKPLIDLALSVSKLKDFTGREKPTVIT | ||||||
Modified residue | 184 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Interaction
Subunit
Monomer.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length626
- Mass (Da)68,575
- Last updated2000-05-01 v1
- ChecksumB820E069AFA0D34E
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ250770 EMBL· GenBank· DDBJ | CAB60128.1 EMBL· GenBank· DDBJ | mRNA |