A0A7Y5Y2K8 · A0A7Y5Y2K8_9BURK
- ProteinThymidylate synthase
- GenethyA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids323 (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 | 21 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 172-173 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: RR | ||||||
Active site | 192 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 214-217 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: RSND | ||||||
Binding site | 217 | (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 225 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: N | ||||||
Binding site | 255-257 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: HIY | ||||||
Binding site | 322 | (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 > Pseudomonadota > Betaproteobacteria > Burkholderiales > Oxalobacteraceae > Herbaspirillum
Accessions
- Primary accessionA0A7Y5Y2K8
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-323 | Thymidylate synthase/dCMP hydroxymethylase | ||||
Sequence: KQYQDLIQDVLENGSWQDNRTGIRTLSIPGAMMRFDLQKGFPAVTTKRLAFKSVVGELCGFLRATRSAADFRALGCKVWDQNANENADWLANPFRTGTDDLGPVYGVQWREWPAYKLIDAAHTAQIDAARAKGFAIVSSLQDKGEEKVLLYKAVDQLRECLDTIVKNPGSRRILFHGWNCAVLDEIALPACHLLYQFLPNQSTGEISLCLYVRSNDIGLGTPFNLAEGAALLHLVARLTGYRPRWFSYFVGDAHIYENHIDMVKEQLTREPYPLPQLAIAERVPEFARTREYAPQWLERVEPSDFSLVNYQHHAPLTAPMAV |
Sequence similarities
Belongs to the thymidylate synthase family. Bacterial-type ThyA subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length323
- Mass (Da)36,512
- Last updated2021-06-02 v1
- ChecksumB59E8FED7808A959