Q2GHW6 · Q2GHW6_EHRCR
- ProteinAmidophosphoribosyltransferase
- GenepurF
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids462 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
Catalytic activity
- 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + L-glutamine + H2O
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Mg2+ ion per subunit.
Note: Binds 1 [4Fe-4S] cluster per subunit.
Pathway
Purine metabolism; IMP biosynthesis via de novo pathway; N1-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 10 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 244 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 293 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 355 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 356 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 392 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 448 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 451 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | amidophosphoribosyltransferase activity | |
Molecular Function | magnesium ion binding | |
Biological Process | 'de novo' IMP biosynthetic process | |
Biological Process | glutamine metabolic process | |
Biological Process | purine nucleobase biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAmidophosphoribosyltransferase
- EC number
- Short namesATase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rickettsiales > Anaplasmataceae > Ehrlichia
Accessions
- Primary accessionQ2GHW6
Proteomes
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-227 | Glutamine amidotransferase type-2 | ||||
Sequence: CGVFAIQNNNCAAINCILGLHALQHRGQESFGIVTSEDNKLHFHYSNEQVNSIFNQQSKIDSLLGNTAIGHIRYSTSGSKVGVQPITLDCKFGKLAIAHNGNLTNAAQIRKSLTERGCIFSSDIDTEVIAHLIAINTENTLLDNVINALKTIKGAYSLVILINGTIICCRDPAGIRPLVLGMLDNSYIVASETCALDIVGAQFIRDVLPGEFITIDQG |
Sequence similarities
In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length462
- Mass (Da)51,026
- Last updated2006-03-21 v1
- Checksum955577165CA9A45A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000236 EMBL· GenBank· DDBJ | ABD45246.1 EMBL· GenBank· DDBJ | Genomic DNA |