A0A7T6Z9D3 · A0A7T6Z9D3_9BACI
- ProteinPhosphoribosylglycinamide formyltransferase
- GenepurN
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids189 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
Catalytic activity
- (6R)-10-formyltetrahydrofolate + N1-(5-phospho-beta-D-ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H+ + N2-formyl-N1-(5-phospho-beta-D-ribosyl)glycinamide
Pathway
Purine metabolism; IMP biosynthesis via de novo pathway; N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide from N1-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 11-13 | N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI) | ||||
Sequence: GSN | ||||||
Binding site | 64 | (6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 89-92 | (6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: MRLL | ||||||
Binding site | 106 | (6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 108 | Proton donor | ||||
Sequence: H | ||||||
Site | 144 | Raises pKa of active site His | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | phosphoribosylglycinamide formyltransferase activity | |
Biological Process | 'de novo' IMP biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphoribosylglycinamide formyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Salicibibacter
Accessions
- Primary accessionA0A7T6Z9D3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-181 | Formyl transferase N-terminal | ||||
Sequence: MRIALFASGTGSNVESILKAIREQKIDAVPVFVFSDRPDASVLEKAKRYEVLTHTFQPRDFDSKQQYEESLLQLLEKNDVQWVILAGYMRLLGATIVEPYAHQIVNIHPSLLPAYPGLDAVGQALDAGAKETGVTIHYVDAGMDTGTVIRQKTVSITTDDTKKSLGEKIKQAEHQLYPETL |
Sequence similarities
Belongs to the GART family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length189
- Mass (Da)21,089
- Last updated2021-09-29 v1
- Checksum3C0AC45DCEE8C9BB
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP054706 EMBL· GenBank· DDBJ | QQK79320.1 EMBL· GenBank· DDBJ | Genomic DNA |