Q0SEI1 · TYSY_RHOJR
- ProteinThymidylate synthase
- GenethyA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids266 (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 | 24 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 54 | (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 129-130 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: RR | ||||||
Active site | 149 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 169-172 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: RSAD | ||||||
Binding site | 172 | (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 180 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: N | ||||||
Binding site | 210-212 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: HIY | ||||||
Binding site | 265 | (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
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Nocardiaceae > Rhodococcus
Accessions
- Primary accessionQ0SEI1
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000000662 | 1-266 | Thymidylate synthase | |||
Sequence: MTVPTPYEDLLRLVMDTGTPKADRTGTGTKSVFGHQMRWNLADGFPLITTKKVHLKSIVYELLWFLRGDSNVKWLQDNGVTIWDEWADADGELGPVYGVQWRSWPTPSGEHIDQITQTIETLKSNPDSRRIIVSAWNVGDIPQMALAPCHAFFQFYVADGKLSCQLYQRSADLFLGVPFNIASYALLTHMVAQQAGLEPGDFIWTGGDCHIYDNHVDQVTEQLSREPLPYPTLKLNKRESIFDYTFEDVEIVDYRHHPAIKAPVAV |
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length266
- Mass (Da)30,152
- Last updated2006-09-05 v1
- Checksum992DB805E90B99E1
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000431 EMBL· GenBank· DDBJ | ABG94055.1 EMBL· GenBank· DDBJ | Genomic DNA |