Q5SKY0 · Q5SKY0_THET8
- ProteinN5-carboxyaminoimidazole ribonucleotide synthase
- GenepurK
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids369 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO3- to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO3- to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
Catalytic activity
- 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP + hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + 2 H+ + phosphate
Pathway
Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 97 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 97 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 137 | AMP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 137 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 142-148 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GYDGKGQ | ||||||
Binding site | 148 | AMP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 172 | AMP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 172-175 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EGFV | ||||||
Binding site | 175 | AMP (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 180 | AMP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 180 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 203 | ATP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 257-258 | ATP (UniProtKB | ChEBI) | ||||
Sequence: NE |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 5-(carboxyamino)imidazole ribonucleotide synthase activity | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | phosphoribosylaminoimidazole carboxylase activity | |
Biological Process | 'de novo' IMP biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameN5-carboxyaminoimidazole ribonucleotide synthase
- EC number
- Short namesN5-CAIR synthase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Deinococcota > Deinococci > Thermales > Thermaceae > Thermus
Accessions
- Primary accessionQ5SKY0
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 101-287 | ATP-grasp | ||||
Sequence: KTFFQGLGVPTPPFHPVDGPEDLEEGLKRVGLPALLKTRRGGYDGKGQALVRTEEEALEALKALGGRGLILEGFVPFDREVSLLAVRGRTGEVAFYPLVENRHWGGILRLSLAPAPGASEALQKKAEAYALRAMEALDYVGVLALEFFQVGEELLFNEMAPRVHNSGHWTIEGAETSQFENHLRAVL |
Sequence similarities
Belongs to the PurK/PurT family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length369
- Mass (Da)40,098
- Last updated2004-12-21 v1
- Checksum2FD069E4369EF34F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP008226 EMBL· GenBank· DDBJ | BAD70336.1 EMBL· GenBank· DDBJ | Genomic DNA |