Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fructose-bisphosphate aldolase

Gene

PF14_0425

Organism
Plasmodium falciparum (isolate 3D7)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (PF14_0341)
  3. Probable ATP-dependent 6-phosphofructokinase (PF3D7_0915400)
  4. Fructose-bisphosphate aldolase (PF14_0425)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei62 – 621SubstrateBy similarity
Binding sitei152 – 1521SubstrateBy similarity
Active sitei195 – 1951Proton acceptorBy similarity
Active sitei237 – 2371Schiff-base intermediate with dihydroxyacetone-PBy similarity
Sitei369 – 3691Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphateBy similarity

GO - Molecular functioni

  • actin binding Source: GeneDB
  • fructose-bisphosphate aldolase activity Source: GeneDB

GO - Biological processi

  • actin polymerization or depolymerization Source: GeneDB
  • glycolytic process Source: GeneDB
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

ReactomeiR-PFA-114608. Platelet degranulation.
R-PFA-70171. Glycolysis.
R-PFA-70263. Gluconeogenesis.
R-PFA-70350. Fructose catabolism.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase (EC:4.1.2.13)
Gene namesi
ORF Names:PF14_0425
OrganismiPlasmodium falciparum (isolate 3D7)
Taxonomic identifieri36329 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)
Proteomesi
  • UP000001450 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiPlasmoDB:PF3D7_1444800.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GeneDB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 369369Fructose-bisphosphate aldolasePRO_0000233386Add
BLAST

PTM databases

SwissPalmiQ7KQL9.

Interactioni

Subunit structurei

Homotetramer.By similarity

GO - Molecular functioni

  • actin binding Source: GeneDB

Protein-protein interaction databases

BioGridi1207364. 4 interactions.
IntActiQ7KQL9. 4 interactions.

Structurei

Secondary structure

1
369
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 2914Combined sources
Beta strandi35 – 395Combined sources
Helixi43 – 5210Combined sources
Helixi59 – 7012Combined sources
Helixi75 – 773Combined sources
Beta strandi79 – 846Combined sources
Helixi86 – 894Combined sources
Beta strandi94 – 963Combined sources
Helixi99 – 1057Combined sources
Beta strandi109 – 1135Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi128 – 1303Combined sources
Helixi136 – 14611Combined sources
Beta strandi150 – 1578Combined sources
Helixi161 – 1633Combined sources
Helixi168 – 18720Combined sources
Beta strandi191 – 1988Combined sources
Helixi206 – 22621Combined sources
Helixi231 – 2333Combined sources
Helixi253 – 26715Combined sources
Beta strandi274 – 2785Combined sources
Helixi284 – 29512Combined sources
Beta strandi301 – 3099Combined sources
Helixi310 – 32011Combined sources
Helixi324 – 3263Combined sources
Helixi327 – 34620Combined sources
Helixi362 – 3665Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4TR9X-ray2.11A/B/C/D1-369[»]
ProteinModelPortaliQ7KQL9.
SMRiQ7KQL9. Positions 4-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000220876.
InParanoidiQ7KQL9.
KOiK01623.
OMAiLEANCRE.
PhylomeDBiQ7KQL9.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view]
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7KQL9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHCTEYMNA PKKLPADVAE ELATTAQKLV QAGKGILAAD ESTQTIKKRF
60 70 80 90 100
DNIKLENTIE NRASYRDLLF GTKGLGKFIS GAILFEETLF QKNEAGVPMV
110 120 130 140 150
NLLHNENIIP GIKVDKGLVN IPCTDEEKST QGLDGLAERC KEYYKAGARF
160 170 180 190 200
AKWRTVLVID TAKGKPTDLS IHETAWGLAR YASICQQNRL VPIVEPEILA
210 220 230 240 250
DGPHSIEVCA VVTQKVLSCV FKALQENGVL LEGALLKPNM VTAGYECTAK
260 270 280 290 300
TTTQDVGFLT VRTLRRTVPP ALPGVVFLSG GQSEEEASVN LNSINALGPH
310 320 330 340 350
PWALTFSYGR ALQASVLNTW QGKKENVAKA REVLLQRAEA NSLATYGKYK
360
GGAGGENAGA SLYEKKYVY
Length:369
Mass (Da):40,105
Last modified:July 5, 2004 - v1
Checksum:i2AE9CDED4F5C96A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014187 Genomic DNA. Translation: AAN37038.1.
RefSeqiXP_001348599.1. XM_001348563.2.

Genome annotation databases

EnsemblProtistsiPF14_0425:mRNA; PF14_0425:pep; PF14_0425.
GeneDBiPF3D7_1444800.1:pep.
GeneIDi812007.
KEGGipfa:PF14_0425.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014187 Genomic DNA. Translation: AAN37038.1.
RefSeqiXP_001348599.1. XM_001348563.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4TR9X-ray2.11A/B/C/D1-369[»]
ProteinModelPortaliQ7KQL9.
SMRiQ7KQL9. Positions 4-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1207364. 4 interactions.
IntActiQ7KQL9. 4 interactions.

PTM databases

SwissPalmiQ7KQL9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiPF14_0425:mRNA; PF14_0425:pep; PF14_0425.
GeneDBiPF3D7_1444800.1:pep.
GeneIDi812007.
KEGGipfa:PF14_0425.

Organism-specific databases

EuPathDBiPlasmoDB:PF3D7_1444800.

Phylogenomic databases

HOGENOMiHOG000220876.
InParanoidiQ7KQL9.
KOiK01623.
OMAiLEANCRE.
PhylomeDBiQ7KQL9.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
ReactomeiR-PFA-114608. Platelet degranulation.
R-PFA-70171. Glycolysis.
R-PFA-70263. Gluconeogenesis.
R-PFA-70350. Fructose catabolism.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view]
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Isolate 3D7.

Entry informationi

Entry nameiALF_PLAF7
AccessioniPrimary (citable) accession number: Q7KQL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: July 5, 2004
Last modified: February 17, 2016
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.