P38972 · PUR4_YEAST
- ProteinPhosphoribosylformylglycinamidine synthase
- GeneADE6
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1358 (go to sequence)
- Protein existenceEvidence at protein level
- 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 (By similarity).
Miscellaneous
Present with 40800 molecules/cell in log phase SD medium.
Catalytic activity
- N2-formyl-N1-(5-phospho-beta-D-ribosyl)glycinamide + L-glutamine + ATP + H2O = 2-formamido-N1-(5-O-phospho-beta-D-ribosyl)acetamidine + L-glutamate + ADP + phosphate + 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 1/2.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 345-356 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GAATGSGGEIRD | ||||||
Binding site | 424-426 | ATP (UniProtKB | ChEBI) | ||||
Sequence: NGY | ||||||
Binding site | 719 | ATP (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 720 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 762 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 766 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 930 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 932 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 1187 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 1319 | |||||
Sequence: H | ||||||
Active site | 1321 | |||||
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
Names & Taxonomy
Protein names
- Recommended namePhosphoribosylformylglycinamidine synthase
- EC number
- Short namesFGAM synthase; FGAMS
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP38972
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylthreonine | ||||
Sequence: T | ||||||
Chain | PRO_0000100405 | 2-1358 | Phosphoribosylformylglycinamidine synthase | |||
Sequence: TDYILPGPKALSQFRVDNLIKDINSYTNSTSVINELRSCYIHYVNGIAQNLSEQDTKLLEVLLTYDSALDIANDPLARQLNDAVANNLPSSALGEDTYLIRVVPRSGTISPWSSKATNIAHVCGLQDKVQRIERGLALLIKTVPGFPLLENLNDISLKCVYDRMTQQLYLTEPPNTMSIFTHEEPKPLVHVPLTPKDTKQSPKDILSKANTELGLALDSGEMEYLIHAFVETMKRDPTDVELFMFAQVNSEHCRHKIFNADWTIDGIKQQFTLFQMIRNTHKLNPEYTISAYSDNAAVLDSENDAFFFAPNSTTKEWTSTKERIPLLIKVETHNHPTAVSPFPGAATGSGGEIRDEGATGRGSKTKCGLSGFSVSDLLIPGNEQPWELNIGKPYHIASALDIMIEAPLGSAAFNNEFGRPCINGYFRTLTTKVLNHQGKEEIRGFHKPIMIAGGFGTVRPQFALKNTPITPGSCLIVLGGQSMLIGLGGGAASSVASGEGSADLDFASVQRGNPEMERRCQQVIDACVALGNNNPIQSIHDVGAGGLSNALPELVHDNDLGAKFDIRKVLSLEPGMSPMEIWCNESQERYVLGVSPQDLSIFEEICKRERAPFAVVGHATAEQKLIVEDPLLKTTPIDLEMPILFGKPPKMSRETITEALNLPEANLSEIPSLQDAIQRVLNLPSVGSKSFLITIGDRSVTGLIDRDQFVGPWQVPVADVGVTGTSLGETIISTGEAMAMGEKPVNALISASASAKLSVAESLLNIFAADVKSLNHIKLSANWMSPASHQGEGSKLYEAVQALGLDLCPALGVAIPVGKDSMSMKMKWDDKEVTAPLSLNITAFAPVFNTSKTWTPLLNRNTDDSVLVLVDLSAKQETKSLGASALLQVYNQVGNKSPTVYDNAILKGFLESLIQLHQQKEDIVLAYHDRSDGGLLITLLEMAFASRCGLEINIDGGDLESQLTNLFNEELGAVFQISAKNLSKFEKILNENGVAKEYISIVGKPSFQSQEIKIINSTTNDVIYANSRSELEQTWSKTSYEMQKLRDNPKTAEEEFASITDDRDPGLQYALTYNPADDMKIGLELSSQRPKVAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLLEGRFHLDDFIGLAACGGFSYGDVLGAGAGWAKSVLYHEGVRSQFSKFFNERQDTFAFGACNGCQFLSRLKDIIPGCENWPSFERNVSEQYEARVCMVQISQEKDNSSEESVFLNGMAGSKLPIAVAHGEGKATFSKSAEQLEKFEKDGLCCIRYVDNYGNVTERFPFNPNGSTNGIAGIKSPNGRVLAMMPHPERVCRLEANSWYPEGKYEEWGGYGPWIRLFRSARRWVG |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 339-363 | Disordered | ||||
Sequence: AVSPFPGAATGSGGEIRDEGATGRG | ||||||
Domain | 1093-1358 | Glutamine amidotransferase type-1 | ||||
Sequence: VAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLLEGRFHLDDFIGLAACGGFSYGDVLGAGAGWAKSVLYHEGVRSQFSKFFNERQDTFAFGACNGCQFLSRLKDIIPGCENWPSFERNVSEQYEARVCMVQISQEKDNSSEESVFLNGMAGSKLPIAVAHGEGKATFSKSAEQLEKFEKDGLCCIRYVDNYGNVTERFPFNPNGSTNGIAGIKSPNGRVLAMMPHPERVCRLEANSWYPEGKYEEWGGYGPWIRLFRSARRWVG |
Sequence similarities
In the N-terminal section; belongs to the FGAMS family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,358
- Mass (Da)148,905
- Last updated1996-10-01 v2
- ChecksumA48A24ECB1BE7973
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 84 | in Ref. 1; AAA50357 | ||||
Sequence: A → L | ||||||
Sequence conflict | 219-220 | in Ref. 1; AAA50357 | ||||
Sequence: DS → EC | ||||||
Sequence conflict | 226 | in Ref. 1; AAA50357 | ||||
Sequence: L → V | ||||||
Sequence conflict | 492 | in Ref. 1; AAA50357 | ||||
Sequence: A → P | ||||||
Sequence conflict | 499 | in Ref. 1; AAA50357 | ||||
Sequence: G → R | ||||||
Sequence conflict | 551 | in Ref. 1; AAA50357 | ||||
Sequence: A → T | ||||||
Sequence conflict | 604 | in Ref. 1; AAA50357 | ||||
Sequence: E → K | ||||||
Sequence conflict | 1169-1170 | in Ref. 1; AAA50357 | ||||
Sequence: SQ → TSSK | ||||||
Sequence conflict | 1298 | in Ref. 1; AAA50357 | ||||
Sequence: G → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U14566 EMBL· GenBank· DDBJ | AAA50357.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z72846 EMBL· GenBank· DDBJ | CAA97063.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006941 EMBL· GenBank· DDBJ | DAA08157.1 EMBL· GenBank· DDBJ | Genomic DNA |