I0BAC6 · I0BAC6_9BACL

  • Protein
    2,3-bisphosphoglycerate-independent phosphoglycerate mutase
  • Gene
    gpmI
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.

Catalytic activity

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 2 manganese ions per subunit.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.

Features

Showing features for binding site, active site.

151450100150200250300350400450500
TypeIDPosition(s)Description
Binding site13Mn2+ 2 (UniProtKB | ChEBI)
Active site63Phosphoserine intermediate
Binding site63Mn2+ 2 (UniProtKB | ChEBI)
Binding site124substrate
Binding site154-155substrate
Binding site186substrate
Binding site192substrate
Binding site262-265substrate
Binding site337substrate
Binding site404Mn2+ 1 (UniProtKB | ChEBI)
Binding site408Mn2+ 1 (UniProtKB | ChEBI)
Binding site445Mn2+ 2 (UniProtKB | ChEBI)
Binding site446Mn2+ 2 (UniProtKB | ChEBI)
Binding site463Mn2+ 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity
Molecular Functionmanganese ion binding
Biological Processglucose catabolic process
Biological Processglycolytic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    2,3-bisphosphoglycerate-independent phosphoglycerate mutase
  • EC number
  • Short names
    BPG-independent PGAM
    ; Phosphoglyceromutase
    ; iPGM

Gene names

    • Name
      gpmI
    • ORF names
      B2K_01020

Organism names

Accessions

  • Primary accession
    I0BAC6

Proteomes

Subcellular Location

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain5-499Metalloenzyme
Domain83-300BPG-independent PGAM N-terminal

Sequence similarities

Belongs to the BPG-independent phosphoglycerate mutase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    514
  • Mass (Da)
    56,304
  • Last updated
    2012-06-13 v1
  • Checksum
    7E0E8A9BD4DF772E
MARPKPVAVIILDGFGLRGDVQGNAVAQAKKPNYERYWNEFPHTTLTACGEAVGLPEGQMGNSEVGHLNIGAGRIVYQDLTRISKSIRDGEFYENETILGAIRHAKDNGKKLHLYGLLSDGGVHSHIEHLFALLDVCKKESFEEVYIHAFLDGRDVAPDSAAGYMERLLKKIADVGVGRIATVQGRYYAMDRDKRWERTEKSYRAMVYGDGPTFEDPMNAIQESYIRSVYDEFVMPTVIVKPDHTPVGLVESGDSVVFFNFRPDRAIQLSQVFTNSDFRGFDRGDKAPTDLYYVCLTLFSETVGGYVAYKPKNLDNTLGEVLAQNDLKQLRIAETEKYPHVTFFFSGGRDVELPGETRILIPSPKVATYDLQPEMSAYELAAAAVAEIEAERQDVIILNFANPDMVGHSGLLEPTIKAVEATDECLGKVVDAIIAKGGVALITADHGNADVVTNPDGSRNTAHTTNPVPFIVTDGRVTLRNDGILADIAPTVLDLLGVSKPAEMTGTTLAASRS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP003422
EMBL· GenBank· DDBJ
AFH59323.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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