Q8I1R6 · Q8I1R6_PLAF7
- ProteinBifunctional dihydrofolate reductase-thymidylate synthase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids608 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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 binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 16 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 40 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 44 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 45 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 106 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 107 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 108 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 111 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 129 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 130 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 166 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 167 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 168 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 169 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 172 | NADPH (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 345 | dUMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 470 | dUMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 471 | dUMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 490 | |||||
Sequence: C | ||||||
Binding site | 490 | dUMP (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 491 | dUMP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 509 | dUMP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 510 | dUMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 511 | dUMP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 513 | dUMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 521 | dUMP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 551 | dUMP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 553 | dUMP (UniProtKB | ChEBI) | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Molecular Function | dihydrofolate reductase activity | |
Molecular Function | nucleotide binding | |
Molecular Function | RNA binding | |
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
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)
Accessions
- Primary accessionQ8I1R6
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Chemistry
PTM/Processing
Proteomic databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-228 | DHFR | ||||
Sequence: DIYAICACCKVESKNEGKKNEVFNNYTFRGLGNKGVLPWKCNSLDMKYFCAVTTYVNESKYEKLKYKRCKYLNKETVDNVNDMPNSKKLQNVVVMGRTSWESIPKKFKPLSNRINVILSRTLKKEDFDEDVYIINKVEDLIVLLGKLNYYKCFIIGGSVVYQEFLEKKLIKKIYFTRINSTYECDVFFPEINENEYQIISVSDVYTSNNTTLDFIIYKK |
Sequence similarities
In the C-terminal section; belongs to the thymidylate synthase family.
In the N-terminal section; belongs to the dihydrofolate reductase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length608
- Mass (Da)71,737
- Last updated2003-03-01 v1
- Checksum26FD4BB4A5F1F4A7
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL844503 EMBL· GenBank· DDBJ | CAD49208.1 EMBL· GenBank· DDBJ | Genomic DNA |