O87796 · ALF_STUST
- ProteinFructose-bisphosphate aldolase
- Genefba
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids354 (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 binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 50 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 83 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 84 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 105 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 142 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 198 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 199 | dihydroxyacetone phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 232 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 233-235 | dihydroxyacetone phosphate (UniProtKB | ChEBI) | ||||
Sequence: GSS | ||||||
Binding site | 275-278 | 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; FBPA
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Stutzerimonas
Accessions
- Primary accessionO87796
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000178726 | 1-354 | Fructose-bisphosphate aldolase | |||
Sequence: MALISMRQMLDHAAEFGYGVPAFNVNNLEQMRAIMEAADKTDSPVIVQASAGARKYAGAPFLRHLILAAIEEFPHIPVCMHQDHGTSPDVCQRSIQLGFSSVMMDGSLREDGKTPADYDYNVRVTQQTVAFAHACGVSVEGELGCLGSLETGMAGEEDGVGAEGVLDHSQLLTDPEEAADFVAKTKVDALAIAIGTSHGAYKFTNPPTGDTLSIQRIKEIHARIPDTHLVMHGSSSVPQEWLKIINEYGGEIGETYGVPVEEIVEGIKYGVRKVNIDTDLRLASTGAIREFLAKNPSEFDPRKYFAKTVAAMRDICIARYEAFGTAGNASKIKPISLEGMFQRYASGELDPKIN |
Structure
Sequence
- Sequence statusComplete
- Length354
- Mass (Da)38,350
- Last updated1998-11-01 v1
- Checksum18922C53CB21A5E9