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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 (PF3D7_1444800), 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)DescriptionActionsGraphical viewLength
Binding sitei62SubstrateBy similarity1
Binding sitei152SubstrateBy similarity1
Active sitei195Proton acceptorBy similarity1
Active sitei237Schiff-base intermediate with dihydroxyacetone-PBy similarity1
Sitei369Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphateBy similarity1

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-6798695. Neutrophil 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)DescriptionActionsGraphical viewLength
ChainiPRO_00002333861 – 369Fructose-bisphosphate aldolaseAdd BLAST369

PTM databases

SwissPalmiQ7KQL9.

Interactioni

Subunit structurei

Homotetramer.By similarity

GO - Molecular functioni

  • actin binding Source: GeneDB

Protein-protein interaction databases

BioGridi1207364. 4 interactors.
IntActiQ7KQL9. 4 interactors.

Structurei

Secondary structure

1369
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 29Combined sources14
Beta strandi35 – 39Combined sources5
Helixi43 – 52Combined sources10
Helixi59 – 70Combined sources12
Helixi75 – 77Combined sources3
Beta strandi79 – 84Combined sources6
Helixi86 – 89Combined sources4
Beta strandi94 – 96Combined sources3
Helixi99 – 105Combined sources7
Beta strandi109 – 113Combined sources5
Beta strandi118 – 120Combined sources3
Beta strandi124 – 126Combined sources3
Beta strandi128 – 130Combined sources3
Helixi136 – 146Combined sources11
Beta strandi150 – 157Combined sources8
Helixi161 – 163Combined sources3
Helixi168 – 187Combined sources20
Beta strandi191 – 198Combined sources8
Helixi206 – 226Combined sources21
Helixi231 – 233Combined sources3
Helixi253 – 267Combined sources15
Beta strandi274 – 278Combined sources5
Helixi284 – 295Combined sources12
Beta strandi301 – 309Combined sources9
Helixi310 – 320Combined sources11
Helixi324 – 326Combined sources3
Helixi327 – 346Combined sources20
Helixi362 – 366Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4TR9X-ray2.11A/B/C/D1-369[»]
E360-366[»]
G358-366[»]
ProteinModelPortaliQ7KQL9.
SMRiQ7KQL9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000220876.
InParanoidiQ7KQL9.
KOiK01623.
OMAiYPPKEIQ.
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

EnsemblProtistsiAAN37038; AAN37038; 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4TR9X-ray2.11A/B/C/D1-369[»]
E360-366[»]
G358-366[»]
ProteinModelPortaliQ7KQL9.
SMRiQ7KQL9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1207364. 4 interactors.
IntActiQ7KQL9. 4 interactors.

PTM databases

SwissPalmiQ7KQL9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiAAN37038; AAN37038; PF14_0425.
GeneDBiPF3D7_1444800.1:pep.
GeneIDi812007.
KEGGipfa:PF14_0425.

Organism-specific databases

EuPathDBiPlasmoDB:PF3D7_1444800.

Phylogenomic databases

HOGENOMiHOG000220876.
InParanoidiQ7KQL9.
KOiK01623.
OMAiYPPKEIQ.
PhylomeDBiQ7KQL9.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
ReactomeiR-PFA-114608. Platelet degranulation.
R-PFA-6798695. Neutrophil 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...

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: November 30, 2016
This is version 81 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.