Q7KQL9 · ALF_PLAF7
- ProteinFructose-bisphosphate aldolase
- GeneFBPA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids369 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a key role in glycolysis by catalyzing the cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate (PubMed:26289816).
Independently of its catalytic activity, connects the actin filaments, and thus the actomyosin motor, to cell surface adhesins of the thrombospondin-related anonymous protein (TRAP), the erythrocyte binding ligand (EBL) and reticulocyte binding homolog (RH) protein families; this interaction is probably involved in transducing the motor force across the parasite surface required for sporozoite and ookinete gliding motility and merozoite invasion (PubMed:22991428, PubMed:25261592) (Probable). Stimulates actin polymerisation (PubMed:25261592).
Independently of its catalytic activity, connects the actin filaments, and thus the actomyosin motor, to cell surface adhesins of the thrombospondin-related anonymous protein (TRAP), the erythrocyte binding ligand (EBL) and reticulocyte binding homolog (RH) protein families; this interaction is probably involved in transducing the motor force across the parasite surface required for sporozoite and ookinete gliding motility and merozoite invasion (PubMed:22991428, PubMed:25261592) (Probable). Stimulates actin polymerisation (PubMed:25261592).
Catalytic activity
- beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Activity regulation
The cytoplasmic tail of TRAP and probably other adhesins acts as a competitive inhibitor as the binding sites of the glycolytic substrate fructose 1,6-bisphosphate and TRAP partially overlap.
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, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 40 | dihydroxyacetone phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 42 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 45 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 49 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 113 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 152 | dihydroxyacetone phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 195 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 195 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 237 | Schiff-base intermediate with dihydroxyacetone phosphate | ||||
Sequence: K | ||||||
Binding site | 237 | dihydroxyacetone phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 279 | dihydroxyacetone phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 279-281 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: SGG | ||||||
Binding site | 280 | dihydroxyacetone phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 307 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 309 | dihydroxyacetone phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 310 | beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 310 | dihydroxyacetone phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Site | 369 | Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | host cell plasma membrane | |
Cellular Component | membrane | |
Molecular Function | actin binding | |
Molecular Function | fructose-bisphosphate aldolase activity | |
Biological Process | actin polymerization or depolymerization | |
Biological Process | glycolytic process | |
Biological Process | protein homotetramerization |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFructose-bisphosphate aldolase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)
Accessions
- Primary accessionQ7KQL9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Peripheral membrane protein
Host cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000233386 | 1-369 | UniProt | Fructose-bisphosphate aldolase | |||
Sequence: MAHCTEYMNAPKKLPADVAEELATTAQKLVQAGKGILAADESTQTIKKRFDNIKLENTIENRASYRDLLFGTKGLGKFISGAILFEETLFQKNEAGVPMVNLLHNENIIPGIKVDKGLVNIPCTDEEKSTQGLDGLAERCKEYYKAGARFAKWRTVLVIDTAKGKPTDLSIHETAWGLARYASICQQNRLVPIVEPEILADGPHSIEVCAVVTQKVLSCVFKALQENGVLLEGALLKPNMVTAGYECTAKTTTQDVGFLTVRTLRRTVPPALPGVVFLSGGQSEEEASVNLNSINALGPHPWALTFSYGRALQASVLNTWQGKKENVAKAREVLLQRAEANSLATYGKYKGGAGGENAGASLYEKKYVY | |||||||
Modified residue (large scale data) | 45 | PTMeXchange | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 129 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 183 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 218 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 315 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 361 | PTMeXchange | Phosphoserine | ||||
Sequence: S |
Proteomic databases
PTM databases
Expression
Developmental stage
Expressed during parasite asexual blood stages, including in schizonts (at protein level).
Interaction
Subunit
Homotetramer (PubMed:26289816).
Interacts with TRAP (via cytoplasmic domain); the interaction prevents substrate binding and thereby inhibits aldolase activity (PubMed:26289816, PubMed:16321976) (Probable). Interacts with MTRAP (via cytoplasmic domain); MTRAP phosphorylation may increase the binding to FBPA (PubMed:16321976).
Interact with RH1 (via cytoplasmic domain) (PubMed:22991428, PubMed:27607074).
Interacts with RH2b (via cytoplasmic domain) (PubMed:22991428, PubMed:27607074).
Interacts with RH4 (via cytoplasmic domain) (PubMed:22991428, PubMed:27607074).
Interacts with AMA1 (via cytoplasmic domain); the interaction is weak, however it may be increased upon AMA1 phosphorylation (PubMed:27607074).
Interacts with EBA140 (via cytoplasmic domain); the interaction is weak (PubMed:27607074).
Interacts with EBA175 (via cytoplasmic domain); the interaction is weak (PubMed:27607074).
Interacts with EBA181 (via cytoplasmic domain); the interaction is weak (PubMed:27607074).
Interacts with G-actin and F-actin (PubMed:25261592).
May interact with ACT2/actin II; the interaction inhibits FBPA catalytic activity (By similarity).
Interacts with human SLC4A1/band 3 (via N-terminus); the interaction inhibits FBPA catalytic activity (By similarity).
Interacts with TRAP (via cytoplasmic domain); the interaction prevents substrate binding and thereby inhibits aldolase activity (PubMed:26289816, PubMed:16321976) (Probable). Interacts with MTRAP (via cytoplasmic domain); MTRAP phosphorylation may increase the binding to FBPA (PubMed:16321976).
Interact with RH1 (via cytoplasmic domain) (PubMed:22991428, PubMed:27607074).
Interacts with RH2b (via cytoplasmic domain) (PubMed:22991428, PubMed:27607074).
Interacts with RH4 (via cytoplasmic domain) (PubMed:22991428, PubMed:27607074).
Interacts with AMA1 (via cytoplasmic domain); the interaction is weak, however it may be increased upon AMA1 phosphorylation (PubMed:27607074).
Interacts with EBA140 (via cytoplasmic domain); the interaction is weak (PubMed:27607074).
Interacts with EBA175 (via cytoplasmic domain); the interaction is weak (PubMed:27607074).
Interacts with EBA181 (via cytoplasmic domain); the interaction is weak (PubMed:27607074).
Interacts with G-actin and F-actin (PubMed:25261592).
May interact with ACT2/actin II; the interaction inhibits FBPA catalytic activity (By similarity).
Interacts with human SLC4A1/band 3 (via N-terminus); the interaction inhibits FBPA catalytic activity (By similarity).
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length369
- Mass (Da)40,105
- Last updated2004-07-05 v1
- Checksum2AE9CDED4F5C96A4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LN999946 EMBL· GenBank· DDBJ | CZU00144.1 EMBL· GenBank· DDBJ | Genomic DNA |