A0A8J7YXW0 · A0A8J7YXW0_9CYAN
- ProteinAmidophosphoribosyltransferase
- GenepurF
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids506 (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
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 | 34 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 278 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 325 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 387 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 388 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 424 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 475 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 478 | [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
Names & Taxonomy
Protein names
- Recommended nameAmidophosphoribosyltransferase
- EC number
- Short namesATase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Leptolyngbyales > Leptolyngbyaceae > Myxacorys > Myxacorys almedinensis
Accessions
- Primary accessionA0A8J7YXW0
Proteomes
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Polar residues | ||||
Sequence: MLPNDPPSDQSACASTPTPETP | ||||||
Region | 1-29 | Disordered | ||||
Sequence: MLPNDPPSDQSACASTPTPETPALSPSDK | ||||||
Domain | 34-262 | Glutamine amidotransferase type-2 | ||||
Sequence: CGVFGVYSPGETVATLAYFGLYALQHRGQESAGIAAFDGNQVNLHKDMGLVSQVFNETILSKLPGALAVGHTRYSTTGSSRVVNAQPAIVPTRLGSLALAHNGNLVNTAQLRAELSQRDHTFITTTDSEMIALALGDEVNDGKSWVDAAASAFQRCSGAFSLVIGTPDGLLGTRDRNGIRPLVLGTLPKDDPELPNRYVLASETCGLDIIGADYVRDIQPGELVWITAE |
Sequence similarities
In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length506
- Mass (Da)54,665
- Last updated2022-05-25 v1
- Checksum92EC910D4BD75FA0
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Polar residues | ||||
Sequence: MLPNDPPSDQSACASTPTPETP |
Keywords
- Technical term