Q8ZCQ2 · PUR4_YERPE
- ProteinPhosphoribosylformylglycinamidine synthase
- GenepurL
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1296 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.
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 binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 306-317 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GAATGSGGEIRD | ||||||
Binding site | 677 | ATP (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 678 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 717 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 721 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 885 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 887 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 1136 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 1261 | |||||
Sequence: H | ||||||
Active site | 1263 | |||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | phosphoribosylformylglycinamidine synthase activity | |
Biological Process | 'de novo' IMP biosynthetic process | |
Biological Process | glutamine metabolic process | |
Biological Process | purine nucleotide biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePhosphoribosylformylglycinamidine synthase
- EC number
- Short namesFGAM synthase ; FGAMS
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Yersiniaceae > Yersinia
Accessions
- Primary accessionQ8ZCQ2
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000100428 | 1-1296 | Phosphoribosylformylglycinamidine synthase | |||
Sequence: MEILRGSPALSAFRITKLLSRCQDAHLLVSDIYAEYVHFADVSAPLSADEHARLQRLLQYGPSLPEHPPAGRLLLVTPRPGTISPWSSKATDIAHNCGLSQILRLERGLAFSIQGPDLNESQWKQLAALLHDRMMEAVFTDLQQAEQLFSHHQPAPVQRVDILGQGRSALEQANIKLGLALAQDEIDYLLTAFTGLGRNPTDIELYMFAQANSEHCRHKIFNADWVIDGVVQPKTLFKMIKNTFEHTPDYVLSAYKDNAAVMEGSQVGRFYATAEKGIYDYHQEEAHILMKVETHNHPTAISPWPGAATGSGGEIRDEGATGRGAKPKAGLVGFSVSNLRIPGFEQPWEENFGKPDRIVTALDIMTEGPLGGAAFNNEFGRPALLGYFRTYEERVNSHNGIELRGYHKPIMLAGGLGNIRADHVQKGEITVGAKLVVLGGPSMNIGLGGGAASSMASGQSDADLDFASVQRDNPEMERRCQEVIDRCWQLGEYNPILFIHDVGAGGLSNAMPELVNDGGRGGRFELRDILNDEPGMSPLEVWCNESQERYVLAVAPAQMALFDEICRRERAPYAVIGEATEEKHLLLNDRHFGNQPIDMPLDVLLGKTPKMLRDVTRLQAKGDALQRADISLAEAVKRIMHLPAVAEKTFLITIGDRTVTGMVTRDQMVGPWQIPVADCAVTSASLDSYYGEAMSLGERAPVALLDFAASARLAVGEALTNIAATQIGELKRIKLSANWMSAAGHPGEDAGLYDAVRAVGEELCPALEITIPVGKDSMSMKTRWQEGHEQREMTSPLSLVITAFARIEDVRRTVTPQLRTDKGDNALLLIDLGAGHNALGATALTQVYRQLGDKPADVRNVQQLAGFFNAMQRLVADQHLLAYHDRSDGGLLVTLAEMAFAGHCGVTVDIQSLGNDALAALFNEELGAVIQVRAEQRADVEKLLADHGLANCVHYLGRAVAGDTFDIRSGTDVVYSEKRSTLRLWWAETSWQMQRLRDNPDCADQEHQAKQDESDPGLNVKLTFDPAEDIAAPFILKQARPKVAVLREQGVNSHVEMAAAFHRAGFDAVDVHMSDLLAGRTDLQSFQTLVACGGFSYGDVLGAGEGWAKSILFNDRVRDEFEAFFHRPTTLALGVCNGCQMMSNLRELIPGAEHWPRFVRNLSDSFEARFSLVEVASSPSLFMQDMVGSRMPIAVSHGEGQVEVRDAAHLAALEQSHLVALRFVNNHGVVTEQYPANPNGSANGITAVTSVSGRATVMMPHPERVFRTVSNSWHPEEWGEDSPWMRMFRNARKQLG |
Proteomic databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 304-323 | Disordered | ||||
Sequence: WPGAATGSGGEIRDEGATGR | ||||||
Compositional bias | 1000-1014 | Basic and acidic residues | ||||
Sequence: PDCADQEHQAKQDES | ||||||
Region | 1000-1019 | Disordered | ||||
Sequence: PDCADQEHQAKQDESDPGLN | ||||||
Domain | 1043-1296 | Glutamine amidotransferase type-1 | ||||
Sequence: VAVLREQGVNSHVEMAAAFHRAGFDAVDVHMSDLLAGRTDLQSFQTLVACGGFSYGDVLGAGEGWAKSILFNDRVRDEFEAFFHRPTTLALGVCNGCQMMSNLRELIPGAEHWPRFVRNLSDSFEARFSLVEVASSPSLFMQDMVGSRMPIAVSHGEGQVEVRDAAHLAALEQSHLVALRFVNNHGVVTEQYPANPNGSANGITAVTSVSGRATVMMPHPERVFRTVSNSWHPEEWGEDSPWMRMFRNARKQLG |
Sequence similarities
In the N-terminal section; belongs to the FGAMS family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,296
- Mass (Da)142,048
- Last updated2002-03-01 v1
- Checksum338EB52821A8888A
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 28 | in Ref. 2; AAM84883 and 3; AAS62733 | ||||
Sequence: L → P | ||||||
Compositional bias | 1000-1014 | Basic and acidic residues | ||||
Sequence: PDCADQEHQAKQDES |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL590842 EMBL· GenBank· DDBJ | CAL21529.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE009952 EMBL· GenBank· DDBJ | AAM84883.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE017042 EMBL· GenBank· DDBJ | AAS62733.1 EMBL· GenBank· DDBJ | Genomic DNA |