A0A1Y3PTF6 · A0A1Y3PTF6_9BACI
- ProteinMultifunctional fusion protein
- GenepurM
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids630 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide: step 2/2.
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 | 448-450 | N1-(5-phospho-beta-D-ribosyl)glycinamide (UniProtKB | ChEBI) | ||||
Sequence: GSN | ||||||
Binding site | 501 | (6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 526-529 | (6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: MRLV | ||||||
Binding site | 543 | (6R)-10-formyltetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 545 | Proton donor | ||||
Sequence: H | ||||||
Site | 581 | Raises pKa of active site His | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | phosphoribosylamine-glycine ligase activity | |
Molecular Function | phosphoribosylformylglycinamidine cyclo-ligase activity | |
Molecular Function | phosphoribosylglycinamide formyltransferase activity | |
Biological Process | 'de novo' IMP biosynthetic process | |
Biological Process | adenine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended namePhosphoribosylformylglycinamidine cyclo-ligase
- EC number
- Alternative names
- Recommended namePhosphoribosylglycinamide formyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionA0A1Y3PTF6
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 66-171 | PurM-like N-terminal | ||||
Sequence: VLVSGSDGVGTKLMLAQALDRHGTIGIDAVAMCVNDVVVQGAEPLFFLDYLALGKVIPEKVEQIVAGVAEGCRQAGCALIGGETAEMPGMYAPEEYDIAGFAVGVA | ||||||
Domain | 183-351 | PurM-like C-terminal | ||||
Sequence: RAGDRLIGLASSGLHSNGFSLVRHLLLEKAGFDLRQPLDELNGRELGEVLLTPTRIYVKTVLRLLERHDIKGMAHITGGGFLENIPRILPPGLGAEIWLGAWPVPPVFRLLQQVGQLSQGECYRTFNMGIGLVLAVAPEEAETVLDAARRLGEEAFLIGQVVPGKGVRL | ||||||
Region | 354-439 | Disordered | ||||
Sequence: GNGNRASDGAGNRATEGSADGGAQGIREGNREGNAEGFRESAGVSTSENRESGATEESGETRESGAAGESGGTGDPGAGSPSPLPR | ||||||
Domain | 439-618 | Formyl transferase N-terminal | ||||
Sequence: RLAVFASGNGSNFQALADACGSGEIPARIALLVTDRPDCTAVERAKRLEIPVLALRPKDFPDKASYERQILNRLQEERVDWVVLAGYMRLVGPTLLSAYEGKMINLHPSLLPAFPGKDAIGQAWRHGVKVTGVTVHFVDEGMDTGPIFLQEPVPVEPGDTLESLEERIHRVEHRLLVEAV |
Sequence similarities
Belongs to the AIR synthase family.
Belongs to the GART family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length630
- Mass (Da)67,250
- Last updated2017-08-30 v1
- Checksum532FD97FD68E47D5