Q9M8D3 · PUR4_ARATH
- ProteinProbable phosphoribosylformylglycinamidine synthase, chloroplastic/mitochondrial
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1407 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Essential to the male gametophyte development. 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 | 407-418 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GAETGAGGRIRD | ||||||
Binding site | 487-489 | ATP (UniProtKB | ChEBI) | ||||
Sequence: QGY | ||||||
Binding site | 786 | ATP (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 787 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 826 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 830 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 989 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 991 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 1235 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 1366 | |||||
Sequence: H | ||||||
Active site | 1368 | |||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | chloroplast stroma | |
Cellular Component | mitochondrion | |
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 | microgametogenesis | |
Biological Process | pollen development |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProbable phosphoribosylformylglycinamidine synthase, chloroplastic/mitochondrial
- EC number
- Short namesFGAM synthase; FGAMS
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9M8D3
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Lethal to the male gametophyte.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 78 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-53 | Chloroplast and mitochondrion | ||||
Sequence: MNTSQATRAALFLNGSNRQAMLLQRSSMSQLWGSVRMRTSRLSLNRTKAVSLR | ||||||
Chain | PRO_0000029880 | 54-1407 | Probable phosphoribosylformylglycinamidine synthase, chloroplastic/mitochondrial | |||
Sequence: CSAQPNKPKAAVSTGSFVTADELPSLVEKPAAEVIHFYRVPLIQESANAELLKAVQTKISNQIVSLTTEQSFNIGLESKLKDEKLSVLKWILQETYEPENLGTDSFLERKKQEGLHAVIVEVGPRLSFTTAWSTNAVSICRACGLDEVTRLERSRRYLLFSKEPLLENQIKEFAAMVHDRMTECVYTQKLVSFETNVVPEEVKYVPVMEKGRKALEEINQEMGLAFDEQDLQYYTRLFREDIKRDPTNVELFDIAQSNSEHSRHWFFAGNMVIDGKPMDKSLMQIVKSTWEANRNNSVIGFKDNSSAIRGFLVNQLRPLLPGSVCLLDVSARDLDILFTAETHNFPCAVAPYPGAETGAGGRIRDTHATGRGSFVVASTSGYCVGNLNMEGSYAPWEDSSFQYPSNLASPLQILIDASNGASDYGNKFGEPMIQGYTRTFGMRLPSGDRREWLKPIMFSAGIGQIDHTHITKGEPEVGMLVVKIGGPAYRIGMGGGAASSMVSGQNDAELDFNAVQRGDAEMSQKLYRVVRACIEMGEKNPIISIHDQGAGGNCNVVKEIIYPQGAEIDIRAVVVGDHTMSVLEIWGAEYQEQDAILVKAESREILQSICKRERLSMAVIGTINGGGRCTLIDSTAAAKCSKEGLPPPPPAVDLELEKVLGDMPKKTFKFNRIAYAREPLDIAPGITLMDALKRVLRLPSVSSKRFLTTKVDRCVTGLVAQQQTVGPLQITLADVAVIAQTFTDLTGGACAIGEQPIKGLLDPKAMARLAVGEALTNLVWAKVTALSDVKASGNWMYAAKLEGEGSAMYDAAIALSEAMIELGIAIDGGKDSLSMAAHADGEVVKAPGNLVISAYVTCPDITKTVTPDLKLGGDDGILLHVDLAKGKRRLGGSALAQVFGQIGNDCPDLDDVPYLKNVFDGVQALIAENLVSAGHDISDGGLVVTALEMAFAGNKGINLDLASNGISLFETLFSEELGLVLEISKTNLDAVMEKLRAFDVTAEIIGNVTDSPLIEVKVDGITHLSEKTSFLRDMWEDTSFQLEKLQRLASCVEMEKEGLKFRHEPNWKLSFIPSSTNNNYMSQDVKPKVAVIREEGSNGDREMSAAFYAAGFEPWDVTVSDLLAGDITLDQFRGIVFVGGFSYADVLDSAKGWAASIRFNEPVLSQFQEFYKRPDTFSLGICNGCQLMALLGWVPGPQVGGSLDTSQPRFVHNESGRFECRFTSVTIKDSPSIMLKGMEGSTLGVWAAHGEGRAYFPDEGVLDHMLHSDLAPLRYCDDDGNVTEAYPFNLNGSPLGIAAICSPDGRHLAMMPHPERCFLMWQFPWYPTSWDVEKAGPSPWLKMFQNARDWLESC |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1141-1381 | Glutamine amidotransferase type-1 | ||||
Sequence: KVAVIREEGSNGDREMSAAFYAAGFEPWDVTVSDLLAGDITLDQFRGIVFVGGFSYADVLDSAKGWAASIRFNEPVLSQFQEFYKRPDTFSLGICNGCQLMALLGWVPGPQVGGSLDTSQPRFVHNESGRFECRFTSVTIKDSPSIMLKGMEGSTLGVWAAHGEGRAYFPDEGVLDHMLHSDLAPLRYCDDDGNVTEAYPFNLNGSPLGIAAICSPDGRHLAMMPHPERCFLMWQFPWYPT |
Sequence similarities
In the N-terminal section; belongs to the FGAMS family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,407
- Mass (Da)153,954
- Last updated2012-06-13 v3
- Checksum49F270F0E2CEBDCB
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
EU091297 EMBL· GenBank· DDBJ | ABW87767.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC020579 EMBL· GenBank· DDBJ | AAG52403.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002684 EMBL· GenBank· DDBJ | AEE35571.1 EMBL· GenBank· DDBJ | Genomic DNA |