A0A2T6IZM3 · A0A2T6IZM3_TOXGO
- ProteinBifunctional dihydrofolate reductase-thymidylate synthase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids610 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.
Catalytic activity
- (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP
Pathway
Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 489 | |||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Molecular Function | dihydrofolate reductase activity | |
Molecular Function | thymidylate synthase activity | |
Biological Process | dTMP biosynthetic process | |
Biological Process | methylation | |
Biological Process | one-carbon metabolic process | |
Biological Process | tetrahydrofolate biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional dihydrofolate reductase-thymidylate synthase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Conoidasida > Coccidia > Eucoccidiorida > Eimeriorina > Sarcocystidae > Toxoplasma
Accessions
- Primary accessionA0A2T6IZM3
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-250 | DHFR | ||||
Sequence: PVCLVVAMTPKRGIGINNGLPWPHLTTDFKHFSRVTKTTPEEASRLNGWLPRKFAKTGDSGLPSPSVGKRFNAVVMGRKTWESMPRKFRPLVDRLNIVVSSSLKEEDIAAEKPQAEGQQRVRVCASLPAALSLLEEEYKDSVDQIFVVGGAGLYEAALSLGVASHLYITRVAREFPCDVFFPAFPGDDILSNKSTAAQAAAPAESVFVPFCPELGREKDNEATYRPIFISKTFSDNGVPYDFVVLEK | ||||||
Region | 256-282 | Disordered | ||||
Sequence: DAATAEPSNAMSSLTSTRETTPVHGLQ | ||||||
Compositional bias | 260-282 | Polar residues | ||||
Sequence: AEPSNAMSSLTSTRETTPVHGLQ |
Sequence similarities
In the C-terminal section; belongs to the thymidylate synthase family.
In the N-terminal section; belongs to the dihydrofolate reductase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length610
- Mass (Da)68,738
- Last updated2018-07-18 v1
- ChecksumCFAF5645CDA04A29
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 260-282 | Polar residues | ||||
Sequence: AEPSNAMSSLTSTRETTPVHGLQ |