A0A533I1D1 · A0A533I1D1_PARDE
- ProteinPhosphoribosylglycinamide formyltransferase
- GenepurN
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids195 (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 | 12-14 | N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI) | ||||
Sequence: GSN | ||||||
Binding site | 65 | (6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 90-93 | (6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: MRIL | ||||||
Binding site | 107 | (6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 109 | Proton donor | ||||
Sequence: H | ||||||
Site | 145 | Raises pKa of active site His | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
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 > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Paracoccaceae > Paracoccus
Accessions
- Primary accessionA0A533I1D1
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-182 | Formyl transferase N-terminal | ||||
Sequence: KRAAILISGGGSNMVKLVESMTGDHPARPVLVGSNDPAAGGLSKARAMGVPVFAVDHRIHGEDRAAFEAELISHLDAVRPDIILLAGFMRILTSDFVRHYEGRMLNIHPSLLPKYPGLHTHARAIEAGDSEAGATVHEVTADLDAGPILGQVKVPVRSGDTPDSLAARVLVQEHRLYPAVL |
Sequence similarities
Belongs to the GART family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length195
- Mass (Da)20,997
- Last updated2019-10-16 v1
- ChecksumE652BA43D80E2DB8