Q2RQK6 · Q2RQK6_RHORT
- ProteinFlavin-dependent thymidylate synthase
- GenethyX
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids285 (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 | 91 | FAD (UniProtKB | ChEBI); ligand shared between neighboring subunits | ||||
Sequence: S | ||||||
Binding site | 112-115 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: ELIR | ||||||
Binding site | 115-117 | FAD (UniProtKB | ChEBI); ligand shared between neighboring subunits | ||||
Sequence: RHR | ||||||
Binding site | 124 | FAD (UniProtKB | ChEBI); ligand shared between neighboring subunits | ||||
Sequence: Q | ||||||
Binding site | 124-128 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: QESQR | ||||||
Binding site | 208 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 224-226 | FAD (UniProtKB | ChEBI); ligand shared between neighboring subunits | ||||
Sequence: NLR | ||||||
Binding site | 230 | FAD (UniProtKB | ChEBI); ligand shared between neighboring subunits | ||||
Sequence: H | ||||||
Active site | 235 | Involved in ionization of N3 of dUMP, leading to its activation | ||||
Sequence: R | ||||||
Binding site | 235 | 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 lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Rhodospirillaceae > Rhodospirillum
Accessions
- Primary accessionQ2RQK6
Proteomes
Interaction
Structure
Sequence
- Sequence statusComplete
- Length285
- Mass (Da)30,689
- Last updated2006-01-24 v1
- Checksum86B7AA39ADECA040
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000230 EMBL· GenBank· DDBJ | ABC23589.1 EMBL· GenBank· DDBJ | Genomic DNA |