A0A5C6LSS4 · A0A5C6LSS4_9BACT
- ProteinFructose-bisphosphate aldolase
- GenefbaA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids355 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.
Catalytic activity
- beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Cofactor
Note: Binds 2 Zn2+ ions per subunit. One is catalytic and the other provides a structural contribution.
Pathway
Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 105 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 106 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 140 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 170 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 222 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 223 | dihydroxyacetone phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 260 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 261-263 | dihydroxyacetone phosphate (UniProtKB | ChEBI) | ||||
Sequence: GGS | ||||||
Binding site | 282-285 | dihydroxyacetone phosphate (UniProtKB | ChEBI) | ||||
Sequence: NLDT |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | fructose-bisphosphate aldolase activity | |
Molecular Function | zinc ion binding | |
Biological Process | gluconeogenesis | |
Biological Process | glycolytic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFructose-bisphosphate aldolase
- EC number
- Short namesFBP aldolase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Chitinophagia > Chitinophagales > Chitinophagaceae > Chitinophaga
Accessions
- Primary accessionA0A5C6LSS4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Sequence
- Sequence statusComplete
- Length355
- Mass (Da)39,231
- Last updated2019-11-13 v1
- Checksum878A050AAC4B4467