About Gene List

PF3D7_1439900 (TIM)

Genome location: Pf3D7_14_v3:1,621,742..1,624,074(+)

Genome classification: Core

Function and Localization

Product Description: triosephosphate isomerase

SignalP Peptide: N/A

# Transmembrane Domains: 0

EC Numbers: 5.3.1.1 (Triose-phosphate isomerase)

Curated GO (PlasmoDB):

Type GO Term Name
Component GO:0005829 cytosol
Function GO:0004807 triose-phosphate isomerase activity
Process GO:0006633 fatty acid biosynthetic process
Process GO:0006094 gluconeogenesis
Process GO:0046166 glyceraldehyde-3-phosphate biosynthetic process
Process GO:0019563 glycerol catabolic process
Process GO:0006096 glycolytic process
Process GO:0006098 pentose-phosphate shunt

Expression by stage (LR - Le Roch et al., and MCA - Malaria Cell Atlas):

Stage LR class MCA mean MCA prop. zeros
Sporozoite expressed N/A N/A
Ring expressed 0.29 0.86
Trophozoite expressed 0.85 0.55
Schizont expressed 0.10 0.93
Gametocyte expressed 0.35 0.80

More info:

Resistome Mutations

Old (Pf3D7v3) Gene ID: PF3D7_1439900

Resistome Missense Mutations: None

Resistome Compounds with Missense Mutations: None

Resistome # Samples with Disruptive Mutations: 0 (0 missense, 0 "interesting" missense)

Essentiality (ABS)

Zhang Phenotype: Non - Mutable in CDS

MIS: 0.122 | MFS: -3.063 | #Insertions: 0

PlasmoGEM Phenotype: Essential (Pb ortholog: PBANKA_1303800)

  • Relative Growth Rate: 0.12 ± 0.13
  • Confidence: 5.40

RMgmDB ABS Phenotype: N/A

More info: PhenoPlasm Link

Binding Evidence

AlphaFill Uniprot ID: Q7KQM0

"Best" AlphaFill ligand hit: 2PG (2-phosphoglyceric acid, Local RMSD=0.04) with 3UWV (Global RMSD=1.86)

BRENDA EC Inhibitors:

EC # Name EC Inhibitors
5.3.1.1 triose-phosphate isomerase ATPNEMPCMBGSSGSO42-AsO2-AsO43-citratesuraminDiamidearsenateAtrazine...

Orthology to BindingDB Entries:

UniProt Protein Name Species Homology Source BindingDB Ligands
P00939 Triosephosphate isomerase Oryctolagus cuniculus OMA, OrthoDB Phosphoglycolohydroxamic AcidCHEMBL195976
P60174 Triosephosphate isomerase OrthoDB Phosphoglycolohydroxamic AcidCHEMBL195976Phosphoglycolohydroxamic Acid

Orthology Information

Ortholog Group (OrthoMCL): OG6_100657

Most Similar Human Ortholog: P60174

TM-align score: 0.96 | RMSD: 1.33

Seq Identity: 0.42 | Length: 247 / 248

All Human Orthologs (OrthoMCL):

Gene ID Description
ENSG00000111669 triosephosphate isomerase 1

Protein Information

Protein Length: 248 | Molecular Weight (kDa): 27.935

UniProt ID(s): A0A144A4G4, Q07412, Q7KQM0

PDB ID(s): None

Isoelectric Point: 6.35

Protein Domain Annotations:

Source Family ID Description
InterPro IPR000652 Triosephosphate isomerase
InterPro IPR020861 Triosephosphate isomerase, active site
InterPro IPR022896 Triosephosphate isomerase, bacterial/eukaryotic
InterPro IPR035990 Triosephosphate isomerase superfamily
PFam PF00121 Triosephosphate isomerase
Superfamily SSF51351 Triosephosphate isomerase superfamily

Genetic Variation

MalariaGEN Pf7 (worldwide samples) # unique SNV/indels:

Homozygous genotype calls only

variant type common rare doubleton singleton
synonymous 5 13 14 22
disruptive 2 18 7 30
missense 2 18 7 28

Any inclusion in genotype call

variant type common rare doubleton singleton
synonymous 8 45 13 18
disruptive 3 52 25 74
missense 3 46 17 47

PlasmoDB Total SNPs: 74

Non-coding: 66 | Synonymous: 4 | Nonsynonymous: 4 | Stop Codon: 0

Associated Publications

PMID Title Authors DOI/Link
7903426 Cloning of the triosephosphate isomerase gene of Plasmodium falciparum andexpression in Escherichia coli. Ranie J, Kumar VP, Balaram H 10.1016/0166-6851(93)90062-3
12368864 Genome sequence of the human malaria parasite Plasmodium falciparum. Gardner MJ, Hall N, ..., Barrell B 10.1038/nature01097
22126412 The structure of the thioredoxin-triosephosphate isomerase complex providesinsights into the reversible glutathione-mediated regulation of triosephosphateisomerase. Shahul HM, Sarma SP 10.1021/bi201224s
26353595 Interaction of Silver Nanoparticles with Triosephosphate Isomerase from Human andMalarial Parasite (Plasmodium falciparum): A Comparative Study. De Moor W, van Marwijk J, Wilhelmi BS, Whiteley CG 10.1166/jbn.2015.2003