Q9SM59 · PGMP_PEA

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).

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

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.

TypeIDPosition(s)Description
Binding site91alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI)
Active site184Phosphoserine intermediate
Binding site184alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI)
Binding site184Mg2+ (UniProtKB | ChEBI); via phosphate group
Binding site349Mg2+ (UniProtKB | ChEBI)
Binding site351Mg2+ (UniProtKB | ChEBI)
Binding site353alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI)
Binding site353Mg2+ (UniProtKB | ChEBI)
Binding site354alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI)
Binding site417alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI)
Binding site436alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI)
Binding site438alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI)
Binding site449alpha-D-glucose 1,6-bisphosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchloroplast
Molecular Functionmagnesium ion binding
Molecular Functionphosphoglucomutase activity
Biological Processglucose metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphoglucomutase, chloroplastic
  • EC number
  • Short names
    PGM
  • Alternative names
    • Glucose phosphomutase

Gene names

    • Name
      PGMP
    • Synonyms
      RUG3

Organism names

  • Taxonomic identifier
  • Strain
    • BC1
  • Taxonomic lineage
    Eukaryota > 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 accession
    Q9SM59

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for transit peptide, chain, modified residue.

TypeIDPosition(s)Description
Transit peptide1-66Chloroplast
ChainPRO_000002389767-626Phosphoglucomutase, chloroplastic
Modified residue184Phosphoserine

Keywords

Interaction

Subunit

Monomer.

Structure

Family & Domains

Sequence similarities

Belongs to the phosphohexose mutase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    626
  • Mass (Da)
    68,575
  • Last updated
    2000-05-01 v1
  • Checksum
    B820E069AFA0D34E
MAFCYRLDNFIISAFKPKHSNVPLSIHHSSSNFPSFKVQNFPFRVRYNSAIRATSSSSSTPTTIAEPNDIKINSIPTKPIEGQKTGTSGLRKKVKVFKQENYLANWIQALFNSLPPEDYKNGLLVLGGDGRYFNKEAAQIIIKIAAGNGVGKILVGKEGILSTPAVSAVIRKREANGGFIMSASHNPGGPEYDWGIKFNYSSGQPAPESITDKIYGNTLSISEIKIADIPDVDLSNVGVTKFGSFSVEVIDPVSDYLELLETVFDFQLIKSLISRPDFRFTFDAMHAVAGAYATPIFVDKLSASLDSISNGIPLEDFGHGHPDPNLTYAKDLVKIMYAENGPDFGAASDGDGDRNMILGTSFFVTPSDSVAVIAANAKEAIPYFKDSIKGLARSMPTSGALDRVAEKLNLPFFEVPTGWKFFGNLMDAGNLSICGEESFGTGSDHIREKDGIWAVLAWLSIIAHRNKDTKPGEKLVSVSDVVKEHWATYGRNFFSRYDYEECESEGANKMIEYLRELLSKSKPGDKYGSYVLQFADDFTYTDPVDGSVVSKQGVRFVFTDGSRIIYRLSGTGSAGATVRVYIEQFEPDVSKHDVDAQIALKPLIDLALSVSKLKDFTGREKPTVIT

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ250770
EMBL· GenBank· DDBJ
CAB60128.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp