A0A292IIU6 · A0A292IIU6_9MOLU

  • 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.

151150100150200250300350400450500
TypeIDPosition(s)Description
Binding site14Mn2+ 2 (UniProtKB | ChEBI)
Active site65Phosphoserine intermediate
Binding site65Mn2+ 2 (UniProtKB | ChEBI)
Binding site126substrate
Binding site155-156substrate
Binding site186substrate
Binding site192substrate
Binding site261-264substrate
Binding site335substrate
Binding site401Mn2+ 1 (UniProtKB | ChEBI)
Binding site405Mn2+ 1 (UniProtKB | ChEBI)
Binding site442Mn2+ 2 (UniProtKB | ChEBI)
Binding site443Mn2+ 2 (UniProtKB | ChEBI)
Binding site460Mn2+ 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
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
      MAMA39_03620

Organism names

Accessions

  • Primary accession
    A0A292IIU6

Proteomes

Subcellular Location

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-496Metalloenzyme
Domain85-298BPG-independent PGAM N-terminal

Sequence similarities

Belongs to the BPG-independent phosphoglycerate mutase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    511
  • Mass (Da)
    56,840
  • Last updated
    2017-12-20 v1
  • Checksum
    D683E6C6367A7B1B
MACNNRKVLLMILDGYGVCKEVKGNAVLNAKTPHLDRLQSAEFPHTLLAASGQAVGLPEGQIGNSEVGHLNIGAGRIIYTGLSLINKAISDHSFYENLALNQAVAHTKKHDSKLHVMGLVSHGGVHSLLNHIVATLKLAHQASVRTVLHIFGDGRDVPPESLLHDLEQLLPTLKELNVTIGMISGRYYAMDRDQRWERIDLAYDALLHGAQITFNDPIQYIKESYAKNESDEFIKPATNAVTDLQTITLQDHDAVVFANFRPDRARQLSHYIYGSNYYQVQPKMRRDGLFFVTMMQYEGIVPSAVAFPPETFKNTLGEVIANAGLKQLRISETEKYAHVTFFFDGGKEVDYPKETKNLIPSNRSVPTYDLVPQMSCKEITDALLPTLGKYELTVLNYANPDMVGHTGKYLPTVQALEMLDVQIGRVIDACIQNNVTLFFTADHGNAEVMLDDKNEPVTKHSTNPVPFTCTDKNIKLLDGGKLANVAPTILDYMEIEIPKEMDEKSILVKNN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HG937516
EMBL· GenBank· DDBJ
CDN40482.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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