Q8ZWV0 · PGMI_PYRAE

Function

function

Catalyzes the isomerization of both glucose 6-phosphate and epimeric mannose 6-phosphate at a similar catalytic efficiency.

Miscellaneous

The lack of any movement in response to the binding of ligand may be due to its inherent thermostability, which would tend to restrict any flexibility in the protein.

Catalytic activity

Activity regulation

Inhibited by 5-phosphoarabinonate (PAB) and 6-phosphogluconate.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
2.7 mMglucose 6-phosphate50
0.3 mMfructose 6-phosphate50
1.9 mMglucose 6-phosphate80
0.06 mMfructose 6-phosphate80
0.49 mMmannose 6-phosphate80
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
50 mmol/min/mg50with glucose 6-phosphate as substrate
31.3 mmol/min/mg50with fructose 6-phosphate as substrate
150 mmol/min/mg80with glucose 6-phosphate as substrate
109 mmol/min/mg80with fructose 6-phosphate as substrate
117 mmol/min/mg80with mannose 6-phosphate as substrate

pH Dependence

Optimum pH is 7.4.

Temperature Dependence

Optimum temperature is 100 degrees Celsius.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site48substrate
Binding site87substrate
Binding site92substrate
Active site203Proton acceptor
Active site219Proton donor
Active site298Proton acceptor

GO annotations

AspectTerm
Molecular Functioncarbohydrate derivative binding
Molecular Functionglucose-6-phosphate isomerase activity
Molecular Functionmannose-6-phosphate isomerase activity
Biological Processcarbohydrate derivative metabolic process
Biological Processcarbohydrate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Bifunctional phosphoglucose/phosphomannose isomerase
  • Alternative names
    • Glucose-6-phosphate isomerase (GPI) (EC:5.3.1.9) . EC:5.3.1.9 (UniProtKB | ENZYME | Rhea)
    • Mannose-6-phosphate isomerase (EC:5.3.1.8) . EC:5.3.1.8 (UniProtKB | ENZYME | Rhea)
    • Phosphoglucose isomerase (PGI)
    • Phosphomannose isomerase (PMI)

Gene names

    • Ordered locus names
      PAE1610

Organism names

Accessions

  • Primary accession
    Q8ZWV0

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002277941-302Bifunctional phosphoglucose/phosphomannose isomerase

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain27-160SIS

Sequence similarities

Belongs to the PGI/PMI family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    302
  • Mass (Da)
    33,548
  • Last updated
    2002-03-01 v1
  • Checksum
    853E7B8E4BA9AA21
MSQLLQDYLNWENYILRRVDFPTSYVVEGEVVRIEAMPRLYISGMGGSGVVADLIRDFSLTWNWEVEVIAVKDYFLKARDGLLIAVSYSGNTIETLYTVEYAKRRRIPAVAITTGGRLAQMGVPTVIVPKASAPRAALPQLLTAALHVVAKVYGIDVKIPEGLEPPNEALIHKLVEEFQKRPTIIAAESMRGVAYRVKNEFNENAKIEPSVEILPEAHHNWIEGSERAVVALTSPHIPKEHQERVKATVEIVGGSIYAVEMHPKGVLSFLRDVGIASVKLAEIRGVNPLATPRIDALKRRLQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE009441
EMBL· GenBank· DDBJ
AAL63599.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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