A1U560 · TPMT_MARN8

Function

Catalytic activity

  • S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.
    EC:2.1.1.67 (UniProtKB | ENZYME | Rhea)

Features

Showing features for binding site.

121920406080100120140160180200
TypeIDPosition(s)Description
Binding site10S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site45S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site66S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site123S-adenosyl-L-methionine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionthiopurine S-methyltransferase activity
Biological Processmethylation
Biological Processresponse to metal ion

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Thiopurine S-methyltransferase
  • EC number
  • Alternative names
    • Thiopurine methyltransferase

Gene names

    • Name
      tpm
    • Ordered locus names
      Maqu_3055

Organism names

Accessions

  • Primary accession
    A1U560

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000472061-219Thiopurine S-methyltransferase

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    219
  • Mass (Da)
    25,493
  • Last updated
    2007-02-06 v1
  • Checksum
    370A45E003976AF0
MEHEFWHERWAKDQIGFHEGTVNQYLHDHWPELAGNGTDAVFVPLCGKAHDMWWLHDRGHPIIGVELSEVACKDFFEEAQEKASVHPGEPFTTFRHDDLQIWCGDYFQLVPDDLKHIRLVYDRAALIALPPEMRKSYVNHLTAIIPDDTRILLITLDYDSSEMQGPPFNVTDDEVFRLYGEDYEINQVLKRDMARDNPFAKRRGLRNGATESVFTLVKK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000514
EMBL· GenBank· DDBJ
ABM20129.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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