Q7N8U4 · TYSY_PHOLL

Function

function

Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.

Catalytic activity

Pathway

Pyrimidine metabolism; dTTP biosynthesis.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site21dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site51(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)
Binding site126-127dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners
Active site146Nucleophile
Binding site166-169dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site169(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)
Binding site177dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site207-209dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site263(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionthymidylate synthase activity
Biological ProcessdTMP biosynthetic process
Biological ProcessdTTP biosynthetic process
Biological Processmethylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Thymidylate synthase
  • EC number
  • Short names
    TS
    ; TSase

Gene names

    • Name
      thyA
    • Ordered locus names
      plu0623

Organism names

Accessions

  • Primary accession
    Q7N8U4

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001410001-264Thymidylate synthase

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    264
  • Mass (Da)
    30,184
  • Last updated
    2003-12-15 v1
  • Checksum
    DE15A59A386CB1C6
MKQYLDLMTRVLAEGTPKADRTGTGTLSIFGHQMRFNLQDGFPLVTTKRCHIRSIIHELLWFLNGDTNIKYLHENGVTIWDEWADENGDLGPVYGKQWRAWGTADGRQIDQLKTVLEQLKSDPDSRRIIVSAWNVGELDKMALAPCHAFFQFYVADGKLSCQLYQRSCDVFLGLPFNIASYALLVHMMAQQCDLEVGDFVWTGGDTHLYSNHMEQTKLQLSREPRSLPKLVIKRKPASLFDYKFDDFEIVDYDPHPGIKAPVAI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BX571861
EMBL· GenBank· DDBJ
CAE12918.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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