P35421 · PUR4_DROME
- ProteinPhosphoribosylformylglycinamidine synthase
- GenePfas
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1354 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway (PubMed:3086869).
Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (PubMed:3086869).
Because of its role in metabolisms, is involved in sleep regulation (PubMed:3086869).
Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (PubMed:3086869).
Because of its role in metabolisms, is involved in sleep regulation (PubMed:3086869).
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 | 327-338 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GATTGTGGRLRD | ||||||
Binding site | 407-409 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SGF | ||||||
Binding site | 714 | ATP (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 715 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 754 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 758 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 918 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 920 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 1180 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 1310 | |||||
Sequence: H | ||||||
Active site | 1312 | |||||
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 nucleobase biosynthetic process | |
Biological Process | purine nucleotide biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphoribosylformylglycinamidine synthase
- EC number
- Short namesFGAM synthase; FGAMS
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP35421
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
Pupal lethal (PubMed:21441212).
RNAi-mediated knockdown in the fat body reduces energy storage of both triglyceride and free glucose, increases waking activity during the day and the night, reduces sleep bout length, with total sleep bout number reduced during the day and increased during the night (PubMed:30249751).
RNAi-mediated knockdown in the fat body reduces energy storage of both triglyceride and free glucose, increases waking activity during the day and the night, reduces sleep bout length, with total sleep bout number reduced during the day and increased during the night (PubMed:30249751).
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000100403 | 1-1354 | Phosphoribosylformylglycinamidine synthase | |||
Sequence: MVILRYYDVQAHSAAEEESVLRRLREEDGAVVSVRMERCYHLEYSAQAEHSLALDELLVWLVKQPLSKGQSLSRQPALQSTGSSQLLLEIGPRFNFSTPYSTNCVNIFQNLGYSEVRRMETSTRYLVTFGEGSKAPEAARFVPLLGDRMTQCLYTEENTPKASFDEQLPERQANWHFVPVLEEGRAALERINQELGLAFNDYDLDYYHDLFAKELGRNPTTVELFDCAQSNSEHSRHWFFRGRMVIDGVEQPKSLIRMIMDTQAHTNPNNTIKFSDNSSAMVGFDHQTIVPSSVVAPGAVRLQSVQSDLIFTAETHNMPTAVAPFSGATTGTGGRLRDVQGVGRGGVPIAGTAGYCVGALHIPGYKQPYEPLDFKYPATFAPPLQVLIEASNGASDYGNKFGEPVISGFALSYGLNSAADASQRDEYVKPIMFSGGLGTMPATMREKLPPARGQLLAKIGGPVYRIGVGGGAASSVEIQGSGDAELDFNAVQRGDAEMENKLNRVVRACLDLGEQNPILAIHDQGAGGNGNVLKELVEPGFAGAVIFSKEFQLGDPTITALELWGAEYQENNAILCNADQRELLEKICRRERCPISFVGVVTGDGRVTLLEKPAPKDLEQALNASNRSEVSPFDLELKYVLGDMPKRTYDLKREQTPLKELSLPKGLLLDEALERVLSLVAVGSKRFLTNKVDRCVGGLIAQQQCVGPLQAPLADYALTTVSHFSHSGIATSIGTQPLKGLLDPAAMARMCVAEALSNLVFVKISELADVKCSGNWMWAAKLPGEGARMFDACKELCQILEELHIAIDGGKDSLSMAAKVGGETIKSPGTLVISTYAPCPDVRLKVTPDLKGPGAGSKTSLLWINLENSARLGGSALAQAYAQQGKDTPNLTRSDVLGKAFAVTQSLLGDGLIQAGHDVSDGGLLVCVLEMAIGGLSGLRVDLSEPLAKLKNFDKSVEKLNRPELAVLFAEECGWVVEVLDTDLERVRSTYEKAGVPNYYLGVTEGFGLDSRVVLKNGKSELLDQPLRVLYKKWERTSYELEKLQANPECAEAEYNSLEYRQAPQYRGPQNVQAELTLKRSSAPVRVAVLREEGVNSEREMMACLLRANFEVHDVTMSDLLQGTASVSQYRGLIFPGGFSYADTLGSAKGWAANILHNPRLLPQFEAFKRRQDVFSLGICNGCQLMTLIGFVGSAKSEVGADPDVALLHNKSQRFECRWATVKIPSNRSIMLGSMKDLVLGCWVAHGEGRFAFRDEKLISHLQSEQLVTLQYVDDVGKPTELYPLNPNGSPQGIAGLCSSDGRHLALMPHPERCSSMYQWPYVPSSFEVSPTQSESPWQIMFNNAYNWCVKSNQ |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1087-1337 | Glutamine amidotransferase type-1 | ||||
Sequence: VAVLREEGVNSEREMMACLLRANFEVHDVTMSDLLQGTASVSQYRGLIFPGGFSYADTLGSAKGWAANILHNPRLLPQFEAFKRRQDVFSLGICNGCQLMTLIGFVGSAKSEVGADPDVALLHNKSQRFECRWATVKIPSNRSIMLGSMKDLVLGCWVAHGEGRFAFRDEKLISHLQSEQLVTLQYVDDVGKPTELYPLNPNGSPQGIAGLCSSDGRHLALMPHPERCSSMYQWPYVPSSFEVSPTQSESP |
Sequence similarities
In the N-terminal section; belongs to the FGAMS family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,354
- Mass (Da)148,085
- Last updated2001-01-11 v2
- Checksum8AA167C2D2920B2C
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 558 | in Ref. 1; AAC46468 | ||||
Sequence: I → Y | ||||||
Sequence conflict | 625 | in Ref. 1; AAC46468 | ||||
Sequence: S → F | ||||||
Sequence conflict | 766 | in Ref. 4; AAR82811 | ||||
Sequence: E → V | ||||||
Sequence conflict | 910 | in Ref. 4; AAR82811 | ||||
Sequence: D → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U00683 EMBL· GenBank· DDBJ | AAC46468.1 EMBL· GenBank· DDBJ | Unassigned DNA | ||
AE014134 EMBL· GenBank· DDBJ | AAF52329.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014134 EMBL· GenBank· DDBJ | AAN10573.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014134 EMBL· GenBank· DDBJ | AAN10574.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT011143 EMBL· GenBank· DDBJ | AAR82811.1 EMBL· GenBank· DDBJ | mRNA |