A0A2W1B4U0 · A0A2W1B4U0_HELAM
- ProteinTriokinase/FMN cyclase
- GeneHaOG213660
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids581 (go to sequence)
- Protein existencePredicted
- Annotation score3/5
Function
function
Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate. Represses IFIH1-mediated cellular antiviral response.
Catalytic activity
- D-glyceraldehyde + ATP = D-glyceraldehyde 3-phosphate + ADP + H+
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | FAD-AMP lyase (cyclizing) activity | |
Molecular Function | glycerone kinase activity | |
Biological Process | glycerol catabolic process | |
Biological Process | phosphorylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTriokinase/FMN cyclase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Lepidoptera > Glossata > Ditrysia > Noctuoidea > Noctuidae > Heliothinae > Helicoverpa
Accessions
- Primary accessionA0A2W1B4U0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Homodimer. Interacts with IFIH1 (via the CARD domains), the interaction is inhibited by viral infection.
Structure
Sequence
- Sequence statusComplete
- Length581
- Mass (Da)61,121
- Last updated2018-09-12 v1
- Checksum65EB307BBC386926
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KZ150341 EMBL· GenBank· DDBJ | PZC71309.1 EMBL· GenBank· DDBJ | Genomic DNA |