A0A8P0NSJ8 · A0A8P0NSJ8_CANLF

Function

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Pathway

Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site67Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site87Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site89Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site90Mg2+ 2 (UniProtKB | ChEBI)
Binding site217Mg2+ 1 (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functioninositol monophosphate 1-phosphatase activity
Molecular Functionmetal ion binding
Biological Processphosphatidylinositol phosphate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Inositol-1-monophosphatase
  • EC number

Gene names

    • Name
      IMPA1

Organism names

Accessions

  • Primary accession
    A0A8P0NSJ8

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the inositol monophosphatase superfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    274
  • Mass (Da)
    29,987
  • Last updated
    2022-10-12 v1
  • MD5 Checksum
    10C4AC3B819A1C4CCAF5D9278ECAF351
MADPWQECMDYAVTLARQVVREAIKNEMNVMIKSSPADLVTATDQKIEKMLLSSIKEKYPSHSFIGEESVAAGEKSILTDSPTWIIDPIDGTTNFVHRFPFVAVSIGFTVNKKMEFGIVYSCLEDKMYTGRKGKGAFCNGQKLQVSQQEDITKSLLVTEFGSSRAPETVRIVLSNLEKLLCIPIHGIRGVGTAAVNMCLVAAGVADAYYEMGIHCWDMAGAGIIVTEAGGVLMDVTGGPFDLMSRRIIAANSKTLAERIAKEIQVIPLQRDDEE

Genome annotation databases

Similar Proteins

Disclaimer

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