A0A0G0W4A4 · A0A0G0W4A4_9BACT
- ProteinMultifunctional fusion protein
- GenethyA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids532 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the deamination of dCTP to dUTP.
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 reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
Catalytic activity
- (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP
Pathway
Pyrimidine metabolism; dTTP biosynthesis.
Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 105-110 | dCTP (UniProtKB | ChEBI) | ||||
Sequence: RSSLAR | ||||||
Binding site | 123 | dCTP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 133 | Proton donor/acceptor | ||||
Sequence: E | ||||||
Binding site | 166 | dCTP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 173 | dCTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 177 | dCTP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Active site | 395 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 415-418 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: RSCD | ||||||
Binding site | 418 | (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 426 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: N | ||||||
Binding site | 456-458 | dUMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: HYY | ||||||
Binding site | 512 | (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | dCTP deaminase activity | |
Molecular Function | nucleotide binding | |
Molecular Function | thymidylate synthase activity | |
Biological Process | dTMP biosynthetic process | |
Biological Process | dTTP biosynthetic process | |
Biological Process | dUMP biosynthetic process | |
Biological Process | dUTP biosynthetic process | |
Biological Process | methylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameThymidylate synthase
- EC number
- Short namesTS ; TSase
- Recommended namedCTP deaminase
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageBacteria
Accessions
- Primary accessionA0A0G0W4A4
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Homotrimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 212-511 | Thymidylate synthase/dCMP hydroxymethylase | ||||
Sequence: QYLNLLQELIDKGHEQVDAGTGVKTYSLFGKQFRFDLSQGFPLLTTKKVFWKGVVQELYWFMSGQKNIKYLVDNNVHIWDDYPYRIYREKITKGLEKEMTKEEFIEKIATDKDFAELHGNLPHVYGDMWRHWPTKTDRTIDQLQWLISNIRNDKSTHSAIVNSWNPEYLYEMAAPGEACRFPICHNMFQINANGGRLSLQLYQRSCDVFLGVPFNIASYALLTIILAKITGNEPGEFIHTFGDIHYYENHLDAVKEQLLREPLPFPTVKIDQNLREIDDFKPESVELIGYESHPPIKASL |
Sequence similarities
Belongs to the dCTP deaminase family.
Belongs to the thymidylate synthase family. Bacterial-type ThyA subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length532
- Mass (Da)60,435
- Last updated2015-07-22 v1
- ChecksumCFCB5DF4D17002BB
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LCBH01000028 EMBL· GenBank· DDBJ | KKS06857.1 EMBL· GenBank· DDBJ | Genomic DNA |