A0A7Y6JTZ9 · A0A7Y6JTZ9_9RICK
- ProteinPhosphoribosylformylglycinamidine synthase subunit PurL
- GenepurL
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids986 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic activity
- ATP + H2O + L-glutamine + N2-formyl-N1-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N1-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H+ + L-glutamate + phosphate
Pathway
Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 253 | |||||
Sequence: H | ||||||
Binding site | 309 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 311 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 313 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 334 | substrate | ||||
Sequence: R | ||||||
Binding site | 335 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 474 | substrate | ||||
Sequence: Q | ||||||
Binding site | 502 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 543-545 | substrate | ||||
Sequence: ESQ | ||||||
Binding site | 736 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 773 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 776 | substrate | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphoribosylformylglycinamidine synthase activity | |
Biological Process | 'de novo' IMP biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphoribosylformylglycinamidine synthase subunit PurL
- EC number
- Short namesFGAM synthase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rickettsiales > Anaplasmataceae > Wolbachieae > Wolbachia
Accessions
- Primary accessionA0A7Y6JTZ9
Proteomes
Subcellular Location
Interaction
Subunit
Monomer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 216-256 | Phosphoribosylformylglycinamidine synthase linker | ||||
Sequence: TLGLSLAAMKAIKDYFNKLGRDPYDIELESLAQTWSEHCKH | ||||||
Domain | 293-422 | PurM-like N-terminal | ||||
Sequence: DNAGGIIFDDDYLIVDKVETHNSPSALDPFGGAMTGALGVNRDILGFGKGAVPIMNTYYFCFAKKAKGKFYRDKERTDEILPPKYIMKEVIHGVNVAGNCSGIPTQLGSVYFDDRFCGKPLVFVGSVGII | ||||||
Domain | 438-586 | PurM-like C-terminal | ||||
Sequence: NGDKIVIIGGRVGRDGIHGATFSSEALSGNSPSTVVQIGDPITQRKLSNAVIQARDLGLYNAITDNGAGGLSSSIGEMGKNGFEVDLSKVPLKNDGMAPWEIWTSESQERMTLAVPEENLPAFKQIMKKHDVEVSVIGKFNESGKAVVK | ||||||
Domain | 699-776 | PurM-like N-terminal | ||||
Sequence: GSSYGEIDTYHMAACAIDTAIRNYVAAGGDINHLALLDNFCWCDAYNPERLWQLKRAAEACYDFATAFQTPFISGKDS | ||||||
Domain | 821-967 | PurM-like C-terminal | ||||
Sequence: PGDLIYVLGITYDELGRSEYQLYSGMGNNNVPKVDAKSARKLYERYNLAIKDGIIASAIAPNLGGSAVALAKSLIAGGLGVEIDLSLVPVGKTQNTDIINKIIMFSESQSRILVTIAPQNQQRFEELFKGIAFSCIGKVTEEKTLNI |
Sequence similarities
Belongs to the FGAMS family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length986
- Mass (Da)108,758
- Last updated2021-06-02 v1
- ChecksumFC68ED8C155FA5EC