A1RQP5 · PURP_PYRIL
- Protein5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase
- GenepurP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids333 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the ATP- and formate-dependent formylation of 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (AICAR) to 5-formaminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (FAICAR) in the absence of folates.
Catalytic activity
- 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + ATP + formate = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide + ADP + phosphate
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 1 Mg2+ or Mn2+ ion per subunit.
Pathway
Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (formate route): step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 20 | 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 85 | 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 136-187 | ATP (UniProtKB | ChEBI) | ||||
Sequence: PEEVDRPVIVKLFGAKGGRGYFLARDREELRRRLAGLSDYIIQEYVFGVPAY | ||||||
Binding site | 209 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 229 | 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 268 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 281 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | ligase activity, forming carbon-nitrogen bonds | |
Molecular Function | magnesium ion binding | |
Biological Process | 'de novo' IMP biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Thermoproteales > Thermoproteaceae > Pyrobaculum
Accessions
- Primary accessionA1RQP5
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000348634 | 1-333 | 5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase | |||
Sequence: MSVLKRYDLEKLAVATVASHTALQILRGAKKYGFRTIAIAGRADVAEFYQQFNFIDEVWTVDFRNFVKAAEKLVEANAVFIPHGSYVEYVGWRQALEAPVPTLGCRELIKWEADQYKKMELLQRGGIPTSRVYKTPEEVDRPVIVKLFGAKGGRGYFLARDREELRRRLAGLSDYIIQEYVFGVPAYYHYFSSPVYGRVEVFGADIRYESNVDGRTFGWVEPTFVVVGNLPLVLRESLLPTIWKYGVQFAKAVEEVVGCRLAGPYCLESIIRDDMSISVFEFSGRIVAGTNIYMGYGSPYSVLYFDRPMDMGERIAHEIREAARRGRLEDLFT |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 106-313 | ATP-grasp | ||||
Sequence: RELIKWEADQYKKMELLQRGGIPTSRVYKTPEEVDRPVIVKLFGAKGGRGYFLARDREELRRRLAGLSDYIIQEYVFGVPAYYHYFSSPVYGRVEVFGADIRYESNVDGRTFGWVEPTFVVVGNLPLVLRESLLPTIWKYGVQFAKAVEEVVGCRLAGPYCLESIIRDDMSISVFEFSGRIVAGTNIYMGYGSPYSVLYFDRPMDMGE |
Sequence similarities
Belongs to the phosphohexose mutase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length333
- Mass (Da)37,993
- Last updated2008-09-02 v2
- ChecksumD0FE1A2EA510D1BE
Sequence caution
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000504 EMBL· GenBank· DDBJ | ABL87277.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |