A1U3I4 · PURT_MARN8
- ProteinFormate-dependent phosphoribosylglycinamide formyltransferase
- GenepurT
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids390 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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
- ATP + formate + N1-(5-phospho-beta-D-ribosyl)glycinamide = ADP + H+ + N2-formyl-N1-(5-phospho-beta-D-ribosyl)glycinamide + phosphateThis reaction proceeds in the forward direction.
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 | 19-20 | N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI) | ||||
Sequence: EL | ||||||
Binding site | 79 | N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 111 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 152 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 157-162 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SSGKGQ | ||||||
Binding site | 192-195 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EGFV | ||||||
Binding site | 200 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 264 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 276 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 283 | N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 353 | N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 360-361 | 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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Marinobacteraceae > Marinobacter
Accessions
- Primary accessionA1U3I4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000319185 | 1-390 | Formate-dependent phosphoribosylglycinamide formyltransferase | |||
Sequence: MGTPLKSNSFRVLFCGSGELGKEVVIELQRFGVEVIAIDRYADAPAMQVAHRSHVVDMLDPVALRSVIEKERPNLIVPEIEAIATPELVKLEQEGYRVIPSARAVNLTMNREGIRRLAAEELGLPTSPYRFAGTREEYLQAVAEVGLPLVVKPVMSSSGKGQSTVKTEADIERAWEYAQTGGRAGKGRVIVEGFVDFDYEITLLTVRHKEGITFCEPIGHRQEDGDYRESWQPQPMNDLALQRSKEIARAVVEDLGGYGIYGVELFVKGENVWFSEVSPRPHDTGLVTLVSQDLSEFAIHARAILGIPVPVVRQNGPSASAVILPEGSSTEVSYTGLEEALAQPGTQLRLFGKPELQGRRRMGVALALGSSIEDAREKARTAASSIKVQF |
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 116-305 | ATP-grasp | ||||
Sequence: RLAAEELGLPTSPYRFAGTREEYLQAVAEVGLPLVVKPVMSSSGKGQSTVKTEADIERAWEYAQTGGRAGKGRVIVEGFVDFDYEITLLTVRHKEGITFCEPIGHRQEDGDYRESWQPQPMNDLALQRSKEIARAVVEDLGGYGIYGVELFVKGENVWFSEVSPRPHDTGLVTLVSQDLSEFAIHARAIL |
Sequence similarities
Belongs to the PurK/PurT family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length390
- Mass (Da)42,705
- Last updated2008-02-26 v2
- Checksum17718B43115E34C2
Sequence caution
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000514 EMBL· GenBank· DDBJ | ABM19553.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |