Q5FR18 · THYX_GLUOX
- ProteinFlavin-dependent thymidylate synthase
- GenethyX
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids303 (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 NADPH and FADH2 as the reductant.
Catalytic activity
- dUMP + (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADPH + H+ = dTMP + (6S)-5,6,7,8-tetrahydrofolate + NADP+
Cofactor
Note: Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.
Pathway
Pyrimidine metabolism; dTTP biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 89 | FAD (UniProtKB | ChEBI); ligand shared between neighboring subunits | |||
Binding site | 109-112 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
Binding site | 112-114 | FAD (UniProtKB | ChEBI); ligand shared between neighboring subunits | |||
Binding site | 120 | FAD (UniProtKB | ChEBI); ligand shared between neighboring subunits | |||
Binding site | 120-124 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | |||
Binding site | 195 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | |||
Binding site | 211-213 | FAD (UniProtKB | ChEBI); ligand shared between neighboring subunits | |||
Binding site | 217 | FAD (UniProtKB | ChEBI); ligand shared between neighboring subunits | |||
Active site | 222 | Involved in ionization of N3 of dUMP, leading to its activation | |||
Binding site | 222 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | NADPH binding | |
Molecular Function | thymidylate synthase (FAD) activity | |
Molecular Function | thymidylate synthase activity | |
Biological Process | dTMP biosynthetic process | |
Biological Process | dTTP biosynthetic process | |
Biological Process | methylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFlavin-dependent thymidylate synthase
- EC number
- Short namesFDTS
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Acetobacteraceae > Gluconobacter
Accessions
- Primary accessionQ5FR18
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000175565 | 1-303 | Flavin-dependent thymidylate synthase | ||
Interaction
Structure
Family & Domains
Features
Showing features for region, domain, motif.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-21 | Disordered | |||
Domain | 43-256 | ThyX | |||
Motif | 112-122 | ThyX motif | |||
Sequence similarities
Belongs to the thymidylate synthase ThyX family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length303
- Mass (Da)34,609
- Last updated2005-03-01 v1
- Checksum98E4392721F9DA72
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000009 EMBL· GenBank· DDBJ | AAW61178.1 EMBL· GenBank· DDBJ | Genomic DNA |