P39771 · PURT_BACSU
- ProteinFormate-dependent phosphoribosylglycinamide formyltransferase
- GenepurT
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids384 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes two reactions: the first one is the production of beta-formyl glycinamide ribonucleotide (GAR) from formate, ATP and beta GAR; the second, a side reaction, is the production of acetyl phosphate and ADP from acetate and ATP.
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 | 14-15 | N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI) | ||||
Sequence: EL | ||||||
Binding site | 74 | N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 106 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 147 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 152-157 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SSGKGQ | ||||||
Binding site | 187-190 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EEFI | ||||||
Binding site | 195 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 259 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 271 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 278 | N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 348 | N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 355-356 | 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 lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionP39771
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000074955 | 1-384 | Formate-dependent phosphoribosylglycinamide formyltransferase | |||
Sequence: MYQSKKVLLLGSGELGKEVVIEAQRLGVQTVAVDSYEHAPAMQVAHNSYVVDMLDPEQIRTIIEKENPDLIVPEVEAIATDELLKLEEEGFHVIPNARAAKLTMDREGIRRLAAETLGLATAGYEFANTYDEFIQAAAQIGFPCVVKPLMSSSGKGQSVCRSEADLESCWETAMEGGRVKNGRVIVEEFIPFESEITLLTVRAVNGTAFCEPIGHVQKDGDYIESWQPHDMTEQQIEEAKHIAKTITDELGGYGLFGVELFLAKDRVYFSEVSPRPHDTGLVTLVTQNLSEFALHVRAILGFPITEITQLSPGASRPLKAPEELADYTVEGLENALAVPKTQVRVFGKPITKAGRRMAVALSAADSVETARENAKKALDQLILK |
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 111-300 | ATP-grasp | ||||
Sequence: RLAAETLGLATAGYEFANTYDEFIQAAAQIGFPCVVKPLMSSSGKGQSVCRSEADLESCWETAMEGGRVKNGRVIVEEFIPFESEITLLTVRAVNGTAFCEPIGHVQKDGDYIESWQPHDMTEQQIEEAKHIAKTITDELGGYGLFGVELFLAKDRVYFSEVSPRPHDTGLVTLVTQNLSEFALHVRAIL |
Sequence similarities
Belongs to the PurK/PurT family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length384
- Mass (Da)42,093
- Last updated1998-12-15 v2
- Checksum5E3642CD6CAF90F7
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 240-241 | in Ref. 1; CAA55557 | ||||
Sequence: KH → ND |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X78962 EMBL· GenBank· DDBJ | CAA55557.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB006424 EMBL· GenBank· DDBJ | BAA33120.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL009126 EMBL· GenBank· DDBJ | CAB12017.1 EMBL· GenBank· DDBJ | Genomic DNA |