A0A099CXV6 · A0A099CXV6_9GAMM
- ProteinAmidophosphoribosyltransferase
- GenepurF
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids491 (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 + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine
Cofactor
Note: Binds 1 Mg2+ ion 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.
GO annotations
Aspect | Term | |
---|---|---|
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
Names & Taxonomy
Protein names
- Recommended nameAmidophosphoribosyltransferase
- EC number
- Short namesATase
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Lysobacterales > Rhodanobacteraceae > Oleiagrimonas
Accessions
- Primary accessionA0A099CXV6
Proteomes
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-234 | Glutamine amidotransferase type-2 | ||||
Sequence: CGIIGIVGTANVASALYDGLTVLQHRGQDAAGIATVDGARLRLHKQKGLVRDVFTQKAMDKLRGHIGIGHCRYPTAGSEDVDEAQPFYVNSPYGIAFAHNGNLVNTEALSREMFEQDRRHINTNSDSEILLNILAHELQIQERMQLTPDHIFKAVAGVHARASGGYACVGLILGYGLVAFRDPHGIRPLVLGERETPNGREYAVASESVALDILGFKFMRDVAPGEAVIISEN |
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
- Length491
- Mass (Da)54,073
- Last updated2015-01-07 v1
- Checksum895D9883ED3B01CB
Keywords
- Technical term