O86262 · TPMT_PSESJ

Function

function

Involved in the biological cycling of tellurium and selenium. Tellurium resistance (Ter) mechanism.

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.

121820406080100120140160180200
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
Biological Processresponse to tellurium ion

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Thiopurine S-methyltransferase
  • EC number
  • Alternative names
    • Tellurite-resistance determinant (TEL-R determinant)
    • Thiopurine methyltransferase

Gene names

    • Name
      tpm

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas > Pseudomonas syringae

Accessions

  • Primary accession
    O86262

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002201291-218Thiopurine S-methyltransferase

Family & Domains

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    218
  • Mass (Da)
    24,446
  • Last updated
    1998-11-01 v1
  • Checksum
    5CD188EA5F9D171F
MKADFWLQRWSAGQIGFHQSEVNKDLQQYWSSLNVVPGARVLVPLCGKSQDMSWLSGQGYHVVGAELSEAAVERYFTERGEQPHITSQGDFKVYAAPGIEIWCGDFFALTARDIGHCAAFYDRAAMIALPADMRERYVQHLEALMPQACSGLLITLEYDQALLEGPPFSVPQTWLHRVMSGNWEVTKVGGQDTLHSSARGLKAGLERMDEHVYVLERV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L49178
EMBL· GenBank· DDBJ
AAC27664.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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