A0A4R3ZCB8 · A0A4R3ZCB8_9ENTR
- ProteinFructose-bisphosphate aldolase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids359 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
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 | 110 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 111 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 145 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 175 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 227 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 228 | dihydroxyacetone phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 265 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 266-268 | dihydroxyacetone phosphate (UniProtKB | ChEBI) | ||||
Sequence: GGS | ||||||
Binding site | 287-290 | dihydroxyacetone phosphate (UniProtKB | ChEBI) | ||||
Sequence: NIDT |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | fructose-bisphosphate aldolase activity | |
Molecular Function | zinc ion binding | |
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 > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Klebsiella/Raoultella group > Raoultella
Accessions
- Primary accessionA0A4R3ZCB8
Proteomes
Structure
Sequence
- Sequence statusComplete
- Length359
- Mass (Da)39,156
- Last updated2019-07-31 v1
- ChecksumA85663466F6F92A1