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P14223 (ALF_PLAFA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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.
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-UniPathway

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

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

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A5CX-ray3.00A/B2-369[»]
2EPHX-ray2.70A/B/C/D1-369[»]
2PC4X-ray2.40A/B/C/D1-369[»]
ProteinModelPortalP14223.
SMRP14223. Positions 4-354.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP14223.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG3588.

Enzyme and pathway databases

UniPathwayUPA00109; UER00183.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERPTHR11627. PTHR11627. 1 hit.
PfamPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14223.

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: October 16, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways