Q7KQL9 · ALF_PLAF7

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).

Catalytic activity

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.

TypeIDPosition(s)Description
Binding site40dihydroxyacetone phosphate (UniProtKB | ChEBI)
Binding site42D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI)
Binding site45D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI)
Binding site49beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI)
Binding site113D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI)
Binding site152dihydroxyacetone phosphate (UniProtKB | ChEBI)
Active site195Proton acceptor
Binding site195D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI)
Active site237Schiff-base intermediate with dihydroxyacetone phosphate
Binding site237dihydroxyacetone phosphate (UniProtKB | ChEBI)
Binding site279dihydroxyacetone phosphate (UniProtKB | ChEBI)
Binding site279-281beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI)
Binding site280dihydroxyacetone phosphate (UniProtKB | ChEBI)
Binding site307beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI)
Binding site309dihydroxyacetone phosphate (UniProtKB | ChEBI)
Binding site310beta-D-fructose 1,6-bisphosphate (UniProtKB | ChEBI)
Binding site310dihydroxyacetone phosphate (UniProtKB | ChEBI)
Site369Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componenthost cell plasma membrane
Cellular Componentmembrane
Molecular Functionactin binding
Molecular Functionfructose-bisphosphate aldolase activity
Biological Processactin polymerization or depolymerization
Biological Processglycolytic process
Biological Processprotein homotetramerization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Fructose-bisphosphate aldolase
  • EC number

Gene names

    • Name
      FBPA
    • ORF names
      PF14_0425, PF3D7_1444800

Organism names

Accessions

  • Primary accession
    Q7KQL9
  • Secondary accessions
    • A0A144A3T1

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Membrane
; Peripheral membrane protein
Host cell membrane
; Peripheral membrane protein

Keywords

PTM/Processing

Features

Showing features for chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00002333861-369UniProtFructose-bisphosphate aldolase
Modified residue (large scale data)45PTMeXchangePhosphothreonine
Modified residue (large scale data)129PTMeXchangePhosphoserine
Modified residue (large scale data)183PTMeXchangePhosphoserine
Modified residue (large scale data)218PTMeXchangePhosphoserine
Modified residue (large scale data)315PTMeXchangePhosphoserine
Modified residue (large scale data)361PTMeXchangePhosphoserine

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).

Protein-protein interaction databases

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    369
  • Mass (Da)
    40,105
  • Last updated
    2004-07-05 v1
  • Checksum
    2AE9CDED4F5C96A4
MAHCTEYMNAPKKLPADVAEELATTAQKLVQAGKGILAADESTQTIKKRFDNIKLENTIENRASYRDLLFGTKGLGKFISGAILFEETLFQKNEAGVPMVNLLHNENIIPGIKVDKGLVNIPCTDEEKSTQGLDGLAERCKEYYKAGARFAKWRTVLVIDTAKGKPTDLSIHETAWGLARYASICQQNRLVPIVEPEILADGPHSIEVCAVVTQKVLSCVFKALQENGVLLEGALLKPNMVTAGYECTAKTTTQDVGFLTVRTLRRTVPPALPGVVFLSGGQSEEEASVNLNSINALGPHPWALTFSYGRALQASVLNTWQGKKENVAKAREVLLQRAEANSLATYGKYKGGAGGENAGASLYEKKYVY

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LN999946
EMBL· GenBank· DDBJ
CZU00144.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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