Q2GH93 · Q2GH93_EHRCR
- ProteinPhosphoribosylglycinamide formyltransferase
- GenepurN
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids208 (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
- N1-(5-phospho-beta-D-ribosyl)glycinamide + (6R)-10-formyltetrahydrofolate = N2-formyl-N1-(5-phospho-beta-D-ribosyl)glycinamide + (6S)-5,6,7,8-tetrahydrofolate + 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 (10-formyl THF route): step 1/1.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 14-16 | N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI) | ||||
Sequence: GSN | ||||||
Binding site | 62 | (6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 104 | (6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 106 | Proton donor | ||||
Sequence: H | ||||||
Site | 142 | 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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rickettsiales > Anaplasmataceae > Ehrlichia
Accessions
- Primary accessionQ2GH93
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-179 | Formyl transferase N-terminal | ||||
Sequence: KLGILISGRGSNMQALINACAQDDFPAEVSCVISNNPKANGLLIAQKQNIKTFVVQGRPLDFDSIDSILRQHQVDLICLAGFMSIVPEGFINKWFHKIINIHPSLLPSFKGLNAQSQALKAGVKIAGCTVHYVYPEVDGGPIIVQAAVPVFSSDNLTDLSERILKMEHICYPKAV |
Sequence similarities
Belongs to the GART family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length208
- Mass (Da)22,811
- Last updated2006-03-21 v1
- Checksum555CA2CFE2600229
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000236 EMBL· GenBank· DDBJ | ABD44645.1 EMBL· GenBank· DDBJ | Genomic DNA |