A0A1Z2TK04 · A0A1Z2TK04_9EURY
- ProteinFormate-dependent phosphoribosylglycinamide formyltransferase
- GenepurT
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids429 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
Catalytic activity
- N1-(5-phospho-beta-D-ribosyl)glycinamide + formate + ATP = N2-formyl-N1-(5-phospho-beta-D-ribosyl)glycinamide + ADP + phosphate + H+
Pathway
Purine metabolism; IMP biosynthesis via de novo pathway; N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide from N1-(5-phospho-D-ribosyl)glycinamide (formate route): step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 26-27 | N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI) | ||||
Sequence: EL | ||||||
Binding site | 86 | N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 118 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 159 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 199-202 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EEHI | ||||||
Binding site | 207 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 276 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 288 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 295 | N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 375 | N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 382-383 | N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI) | ||||
Sequence: RR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | ligase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphoribosylglycinamide formyltransferase 2 activity | |
Molecular Function | phosphoribosylglycinamide formyltransferase activity | |
Biological Process | 'de novo' IMP biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFormate-dependent phosphoribosylglycinamide formyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Thermococci > Thermococcales > Thermococcaceae > Thermococcus
Accessions
- Primary accessionA0A1Z2TK04
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 123-319 | ATP-grasp | ||||
Sequence: ETLAKEAKVPTSRYAYATTLDELYEACERIGYPCHTKAIMSSSGKGSYFVKGPEDVPKAWEVAKKKARGSADKIIVEEHIDFDVEITELAVRHYDENGEVVTTFPRPVGHYQIDGDYHASWQPAEISEKAEREVYRIAKRITDVLGGLGLFGVEMFVKGDRVWANEVSPRPHDTGMVTLASHPTGFSEFGLHLRAVL |
Sequence similarities
Belongs to the PurK/PurT family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length429
- Mass (Da)48,058
- Last updated2017-09-27 v1
- Checksum2FF5705E34054032
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP021848 EMBL· GenBank· DDBJ | ASA76770.1 EMBL· GenBank· DDBJ | Genomic DNA |