A0A9D8TE67 · A0A9D8TE67_9BACT
- ProteinMultifunctional fusion protein
- GenenadA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids506 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic activity
- H2O + ITP = diphosphate + H+ + IMP
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Mg2+ ion per subunit.
Note: Binds 1 [4Fe-4S] cluster per subunit.
Pathway
Cofactor biosynthesis; NAD+ biosynthesis; quinolinate from iminoaspartate: step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 23 | iminosuccinate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 40 | iminosuccinate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 85 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 111-113 | iminosuccinate (UniProtKB | ChEBI) | ||||
Sequence: YVN | ||||||
Binding site | 128 | iminosuccinate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 171 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 197-199 | iminosuccinate (UniProtKB | ChEBI) | ||||
Sequence: HPE | ||||||
Binding site | 214 | iminosuccinate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 264 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 320-325 | substrate | ||||
Sequence: THNAHK | ||||||
Active site | 381 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 381 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 382 | substrate | ||||
Sequence: T | ||||||
Binding site | 461-464 | substrate | ||||
Sequence: FGYD | ||||||
Binding site | 484 | substrate | ||||
Sequence: K | ||||||
Binding site | 489-490 | substrate | ||||
Sequence: HR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | metal ion binding | |
Molecular Function | nucleoside triphosphate diphosphatase activity | |
Molecular Function | nucleotide binding | |
Molecular Function | quinolinate synthetase A activity | |
Molecular Function | ribonucleoside triphosphate phosphatase activity | |
Biological Process | NAD biosynthetic process | |
Biological Process | purine nucleoside triphosphate catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended namedITP/XTP pyrophosphatase
- EC number
- Alternative names
- Recommended nameQuinolinate synthase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Bacteroidia > Bacteroidales
Accessions
- Primary accessionA0A9D8TE67
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Sequence similarities
Belongs to the HAM1 NTPase family.
Belongs to the quinolinate synthase family. Type 2 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length506
- Mass (Da)56,095
- Last updated2023-05-03 v1
- ChecksumD2416BFE29AE3BEB
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: E |