A0A0K9G871 · A0A0K9G871_9BACI
- ProteinFructose-bisphosphate aldolase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids285 (go to sequence)
- Protein existencePredicted
- Annotation score1/5
Function
Cofactor
Note: Binds 2 Zn2+ ions per subunit. One is catalytic and the other provides a structural contribution.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 85 | Proton donor | |||
Binding site | 86 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 107 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 137 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 181 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 182 | dihydroxyacetone phosphate (UniProtKB | ChEBI) | |||
Binding site | 209 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 210-212 | dihydroxyacetone phosphate (UniProtKB | ChEBI) | |||
Binding site | 231-234 | dihydroxyacetone phosphate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | fructose-bisphosphate aldolase activity | |
Molecular Function | zinc ion binding | |
Biological Process | fructose 1,6-bisphosphate metabolic process | |
Biological Process | glycolytic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionA0A0K9G871
Proteomes
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length285
- Mass (Da)30,566
- Last updated2015-11-11 v1
- ChecksumFD230B257AE5B11E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LFZV01000001 EMBL· GenBank· DDBJ | KMY42939.1 EMBL· GenBank· DDBJ | Genomic DNA |