A0A1M7T6N4 · A0A1M7T6N4_9BACT
- ProteinAmidophosphoribosyltransferase
- GenepurF
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids455 (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 | 5 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 246 | [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 | 442 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 445 | [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
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfovibrionia > Desulfovibrionales > Desulfovibrionaceae > Desulfovibrio
Accessions
- Primary accessionA0A1M7T6N4
Proteomes
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-225 | Glutamine amidotransferase type-2 | ||||
Sequence: CGIMGVYNHTEATKLVYFGLYAQQHRGQESAGITAWDGTKISDKRVFGLASSNFTENDFISNLKGHIAIGHVSSKPEKQAFLSCVDPFIIKYKGTTMVAALNGGLTNSQELRDLLENDGGVLRSDSDSELFLHLIVRNLHTMSEEQAVLAAARQLKGAFSFLLMIKNRIYVVRDTFGFKPLALAQYGESIIIASETCAFDLIEAKYIRDVEPGEVLIIDEK |
Sequence similarities
In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length455
- Mass (Da)50,996
- Last updated2017-03-15 v1
- Checksum800B5EB1A8DEA78B
Keywords
- Technical term