A0A8T5QDP8 · A0A8T5QDP8_9ARCH
- ProteinMultifunctional fusion protein
- GenepurD
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids891 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
Catalytic activity
- 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H+ + N1-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
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.
Purine metabolism; IMP biosynthesis via de novo pathway; N1-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 2 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 240 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 288 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 350 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 351 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 387 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 435 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 438 | [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 | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphoribosylamine-glycine ligase activity | |
Biological Process | 'de novo' IMP biosynthetic process | |
Biological Process | glutamine metabolic process | |
Biological Process | purine nucleobase biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended namePhosphoribosylamine--glycine ligase
- EC number
- Alternative names
- Recommended nameAmidophosphoribosyltransferase
- EC number
- Short namesATase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Candidatus Woesearchaeota
Accessions
- Primary accessionA0A8T5QDP8
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-223 | Glutamine amidotransferase type-2 | ||||
Sequence: CGIIGVINKEGEVFENIVVGLISLQHRGQDACGIITNQGEEFLIKKEIDPVHRVFSESDANKLKGRIGIGHTRYATQGRGALSDIQPLSTKTLPKIAMAHNGNAINYFELKEEFLKQGYKLETTVDSELILKIFAYKYQKNKDFFESAKEVFEKVKGSYALVGVIADKGLFAIRDPHGIRPLVLGKKGNSYMVASETVAFQVSDYEFVRDIAPGEALFISKD | ||||||
Domain | 576-781 | ATP-grasp | ||||
Sequence: RRFMHKYNLPSVEFREFTDFSEAEKYIKEKGAPIVVKADGLAAGKGAFVANTEEEAVDFAKECLINNRFGQASSKIIVEECLIGEEASYLVFMDSETFSPMVYSQDHKPVFEGDKGPNTGGMGAYSPAPILDSHEKELEEKIIKPFLKGIKQEGIDFKGVLYVGLMKTNRGLKILEFNCRFGDPETQIILPRLKTDIIDVMNAVID |
Sequence similarities
Belongs to the GARS family.
In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length891
- Mass (Da)98,995
- Last updated2022-10-12 v1
- Checksum9774EE91623147F4