P83155 (ALF_ANASL) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 9, 2013.
Version 24.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Fructose-bisphosphate aldolase Short name=FBP aldolase Short name=FBPA EC=4.1.2.13 Alternative name(s): Fructose-1,6-bisphosphate aldolase |
| Organism | Anabaena sp. (strain L31) |
| Taxonomic identifier | 29412 [NCBI] |
| Taxonomic lineage | Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Anabaena![]() |
Protein attributes
| Sequence length | 16 AA. |
| Sequence status | Fragment. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| 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 By similarity. |
| Catalytic activity | D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. UniProtKB P29271 |
| Cofactor | Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution By similarity. |
| Pathway | Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. UniProtKB P29271 |
| Subunit structure | Homodimer By similarity. UniProtKB P29271 |
| Sequence similarities | Belongs to the class II fructose-bisphosphate aldolase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Ligand | Metal-binding Zinc |
| Molecular function | Lyase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Molecular_function | fructose-bisphosphate aldolase activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | Apte S.K., Uhlemann E., Schmid R., Altendorf K. Submitted (OCT-2001) to UniProtKB Cited for: PROTEIN SEQUENCE. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| UniPathway | UPA00109; UER00183. |
Family and domain databases | |
| PROSITE | PS00602. ALDOLASE_CLASS_II_1. Partial match. PS00806. ALDOLASE_CLASS_II_2. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ALF_ANASL | ||||||||
| Accession | Primary (citable) accession number: P83155 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
