Q9UZ51 · THYX_PYRAB
- ProteinFlavin-dependent thymidylate synthase
- GenethyX
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids244 (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
- (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H+ + NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + 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 | 56 | FAD (UniProtKB | ChEBI); ligand shared between neighboring subunits | ||||
Sequence: S | ||||||
Binding site | 77-80 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: QLVR | ||||||
Binding site | 80-82 | FAD (UniProtKB | ChEBI); ligand shared between neighboring subunits | ||||
Sequence: RHR | ||||||
Binding site | 88 | FAD (UniProtKB | ChEBI); ligand shared between neighboring subunits | ||||
Sequence: Q | ||||||
Binding site | 88-92 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: QQSQR | ||||||
Binding site | 146 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 162-164 | FAD (UniProtKB | ChEBI); ligand shared between neighboring subunits | ||||
Sequence: NLR | ||||||
Binding site | 168 | FAD (UniProtKB | ChEBI); ligand shared between neighboring subunits | ||||
Sequence: H | ||||||
Active site | 173 | Involved in ionization of N3 of dUMP, leading to its activation | ||||
Sequence: R | ||||||
Binding site | 173 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | thymidylate synthase (FAD) 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 lineageArchaea > Euryarchaeota > Thermococci > Thermococcales > Thermococcaceae > Pyrococcus
Accessions
- Primary accessionQ9UZ51
- Secondary accessions
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000175591 | 1-244 | Flavin-dependent thymidylate synthase | |||
Sequence: MVRVTLVNYTRRPLETITWAALVSYWDEWSTESFEKINEDDVKAHLPRILGYGHESILEHATFTFSIEGCSRVCTHQLVRHRIASYTQQSQRYIVLNEENVEETFVIPESIKKDRELYEKWKKAMAETIKLYKESLKRGIHQEDARFILPQAVRSKIVVTMNLRELKHFFGLRLCERAQWEIREVAWKMLEEIAKREELRPIIKWAKLGPRCIQLGYCPERELMPPGCFKRTRERWMKLLEKPL |
Interaction
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-207 | ThyX | ||||
Sequence: VRVTLVNYTRRPLETITWAALVSYWDEWSTESFEKINEDDVKAHLPRILGYGHESILEHATFTFSIEGCSRVCTHQLVRHRIASYTQQSQRYIVLNEENVEETFVIPESIKKDRELYEKWKKAMAETIKLYKESLKRGIHQEDARFILPQAVRSKIVVTMNLRELKHFFGLRLCERAQWEIREVAWKMLEEIAKREELRPIIKWAK | ||||||
Motif | 80-90 | ThyX motif | ||||
Sequence: RHRIASYTQQS |
Sequence similarities
Belongs to the thymidylate synthase ThyX family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length244
- Mass (Da)29,193
- Last updated2000-05-01 v1
- ChecksumBD54D9AB170222BD
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ248287 EMBL· GenBank· DDBJ | CAB50208.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
HE613800 EMBL· GenBank· DDBJ | CCE70744.1 EMBL· GenBank· DDBJ | Genomic DNA |