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Reviewed, UniProtKB/Swiss-Prot P14223 (ALF_PLAFA)

Last modified June 16, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Fructose-bisphosphate aldolase
    EC=4.1.2.13
Alternative name(s):
    41 kDa antigen
OrganismPlasmodium falciparum
Taxonomic identifier5833 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandSchiff base
   Molecular functionLyase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369Fructose-bisphosphate aldolase
PRO_0000216930

Sites

Active site1951Proton acceptor By similarity
Active site2371Schiff-base intermediate with dihydroxyacetone-P
Binding site621Substrate
Binding site1521Substrate
Site3691Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

Secondary structure

................................................... 369
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14223-1 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 2AE9CDED4F5C96A4

FASTA36940,105
        10         20         30         40         50         60 
MAHCTEYMNA PKKLPADVAE ELATTAQKLV QAGKGILAAD ESTQTIKKRF DNIKLENTIE 

        70         80         90        100        110        120 
NRASYRDLLF GTKGLGKFIS GAILFEETLF QKNEAGVPMV NLLHNENIIP GIKVDKGLVN 

       130        140        150        160        170        180 
IPCTDEEKST QGLDGLAERC KEYYKAGARF AKWRTVLVID TAKGKPTDLS IHETAWGLAR 

       190        200        210        220        230        240 
YASICQQNRL VPIVEPEILA DGPHSIEVCA VVTQKVLSCV FKALQENGVL LEGALLKPNM 

       250        260        270        280        290        300 
VTAGYECTAK TTTQDVGFLT VRTLRRTVPP ALPGVVFLSG GQSEEEASVN LNSINALGPH 

       310        320        330        340        350        360 
PWALTFSYGR ALQASVLNTW QGKKENVAKA REVLLQRAEA NSLATYGKYK GGAGGENAGA 


SLYEKKYVY 

« Hide

References

[1]"A new blood stage antigen of Plasmodium falciparum transported to the erythrocyte surface."
Knapp B., Hundt E., Kuepper H.A.
Mol. Biochem. Parasitol. 37:47-56(1989) [PubMed: 2693962] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Plasmodium falciparum aldolase: gene structure and localization."
Knapp B., Hundt E., Kuepper H.A.
Mol. Biochem. Parasitol. 40:1-12(1990) [PubMed: 2190085] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Crystal structure of fructose-1,6-bisphosphate aldolase from the human malaria parasite Plasmodium falciparum."
Kim H., Certa U., Dobeli H., Jakob P., Hol W.G.J.
Biochemistry 37:4388-4396(1998) [PubMed: 9521758] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

M28881 Genomic DNA. Translation: AAA29473.1.
A13461 Unassigned DNA. Translation: CAA01107.1.
A13481 Unassigned DNA. Translation: CAA01117.1.
PIRA44942.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1A5CX-ray3.00A/B2-369[»]
2EPHX-ray2.70A/B/C/D1-369[»]
2PC4X-ray2.40A/B/C/D1-369[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.1.2.13. 1455.

Family and domain databases

InterProIPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR11627. Aldolase_I. 1 hit.
PfamPF00274. Glycolytic. 1 hit.
[Graphical view]
ProDomPD001128. Aldolase_I. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF_PLAFA
AccessionPrimary (citable) accession number: P14223
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents