A2SHH0 · TYSY_METPP
- ProteinThymidylate synthase
- GenethyA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids283 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
- (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP
Pathway
Pyrimidine metabolism; dTTP biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 33 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 63 | (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 138-139 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: RR | ||||||
Active site | 158 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 185-188 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: RSAD | ||||||
Binding site | 188 | (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 196 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: N | ||||||
Binding site | 226-228 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: HIY | ||||||
Binding site | 282 | (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: A |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | thymidylate synthase activity | |
Biological Process | dTMP biosynthetic process | |
Biological Process | dTTP biosynthetic process | |
Biological Process | methylation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameThymidylate synthase
- EC number
- Short namesTS ; TSase
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Sphaerotilaceae > Methylibium
Accessions
- Primary accessionA2SHH0
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000321471 | 1-283 | Thymidylate synthase | |||
Sequence: MSALPSPSPRPARSQYEDFLRHVRDHGVVKADRTGTGTTSVFGHQMRFDLREGFPLVTTKKVHLKSIVLELLWFLRGDGNATWLQERGVTIWDEWAAPDGDLGPVYGVQWRSWPTPDGGHVDQIAEVVKQLKTNPDSRRIIVSAWNVADLPKMALMPCHAFFQFYVAPGDSPSARGRLSCQLYQRSADIFLGVPFNIASYALLTHMLAQQCDLEVGDFVWTGGDCHIYSNHREQVELQLSRAPRPYPTLQIKRRPPSIFDYAYEDFEIIGYDPHPAIKAPVAV |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length283
- Mass (Da)31,957
- Last updated2007-03-06 v1
- Checksum336F46A78B742935
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000555 EMBL· GenBank· DDBJ | ABM95009.1 EMBL· GenBank· DDBJ | Genomic DNA |