A0A5N9E0H8 · A0A5N9E0H8_9CHLR
- ProteindTTP/UTP pyrophosphatase
- GenerlmD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids738 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic activity
- H2O + UTP = diphosphate + H+ + UMP
Cofactor
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 329 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 358 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 379 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 422 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 449 | |||||
Sequence: C | ||||||
Active site | 449 | Nucleophile | ||||
Sequence: C | ||||||
Site | 531 | Important for substrate specificity | ||||
Sequence: R | ||||||
Active site | 588 | Proton acceptor | ||||
Sequence: D | ||||||
Site | 589 | Important for substrate specificity | ||||
Sequence: S | ||||||
Site | 673 | Important for substrate specificity | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | dTTP diphosphatase activity | |
Molecular Function | rRNA (uridine-C5-)-methyltransferase activity | |
Molecular Function | UTP diphosphatase activity | |
Biological Process | nucleotide metabolic process | |
Biological Process | rRNA base methylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namedTTP/UTP pyrophosphatase
- EC number
- Short namesdTTPase/UTPase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Chloroflexota > Dehalococcoidia > SAR202 cluster
Accessions
- Primary accessionA0A5N9E0H8
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 101-159 | TRAM | ||||
Sequence: ITQQGDRVTLSLTSWGRLGEAMAEFDGHNVFVAGGIPGEKVVAEVVKVHRKYVSAKVVA | ||||||
Region | 494-525 | Disordered | ||||
Sequence: QPNEPMAGTITSRAPEPTLETEPESADPPITL | ||||||
Compositional bias | 497-511 | Polar residues | ||||
Sequence: EPMAGTITSRAPEPT |
Sequence similarities
Belongs to the Maf family. YhdE subfamily.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length738
- Mass (Da)80,367
- Last updated2020-04-22 v1
- Checksum09F5B23BC2B6F5E4
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 497-511 | Polar residues | ||||
Sequence: EPMAGTITSRAPEPT |