About Gene List

PF3D7_1116200 (PDX2)

Genome location: Pf3D7_11_v3:615,730..617,191(-)

Genome classification: Core

Function and Localization

Product Description: pyridoxine biosynthesis protein PDX2

SignalP Peptide: N/A

# Transmembrane Domains: 0

EC Numbers: 1.4.3.5 (Pyridoxal 5'-phosphate synthase);3.5.1.2 (Glutaminase);4.3.3.6 (Pyridoxal 5'-phosphate synthase (glutamine hydrolyzing))

Curated GO (PlasmoDB):

Type GO Term Name
Component GO:0005829 cytosol
Component GO:1903600 glutaminase complex
Function GO:0004359 glutaminase activity
Process GO:0042823 pyridoxal phosphate biosynthetic process
Process GO:0008614 pyridoxine metabolic process
Process GO:0000304 response to singlet oxygen
Process GO:0042819 vitamin B6 biosynthetic process

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

Stage LR class MCA mean MCA prop. zeros
Sporozoite not expressed N/A N/A
Ring not expressed nd nd
Trophozoite not expressed nd nd
Schizont not expressed nd nd
Gametocyte not expressed nd nd

More info:

Resistome Mutations

Old (Pf3D7v3) Gene ID: PF3D7_1116200.2

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: 0.861 | MFS: -2.264 | #Insertions: 0

PlasmoGEM Phenotype: N/A

RMgmDB ABS Phenotype: N/A

More info: PhenoPlasm Link

Binding Evidence

AlphaFill Uniprot ID: A0A144A0A4

"Best" AlphaFill ligand hit: No AlphaFill hits

BRENDA EC Inhibitors:

EC # Name EC Inhibitors
1.4.3.5 pyridoxal 5'-phosphate synthase Phenylglyoxal2,3-Butanedione2,4-pentandioneammonium sulfatediethyldicarbonatepyridoxal 5'-phosphate4-chloromercuribenzoatepyridoxine 5'-phosphatecitrate-phosphate bufferpyridoxamine 5'-phosphate4-Pyridoxic acid phosphatepyridoxaloxime 5'-phosphate...
3.5.1.2 glutaminase NH3NEMNaFNaIEDTANH4+PCMBTLCKHgCl2MgCl2CaCl2CuSO4...
4.3.3.6 pyridoxal 5'-phosphate synthase (glutamine hydrolysing) acivicinD-erythroseD-erythronhydrazideD-erythrose 4-phosphate2-deoxy-D-ribose 5-phosphate4-phospho-D-erythronhydrazide
1.4.3.5 pyridoxal 5'-phosphate synthase Phenylglyoxal2,3-Butanedione2,4-pentandioneammonium sulfatediethyldicarbonatepyridoxal 5'-phosphate4-chloromercuribenzoatepyridoxine 5'-phosphatecitrate-phosphate bufferpyridoxamine 5'-phosphate4-Pyridoxic acid phosphatepyridoxaloxime 5'-phosphate...
3.5.1.2 glutaminase NH3NEMNaFNaIEDTANH4+PCMBTLCKHgCl2MgCl2CaCl2CuSO4...
4.3.3.6 pyridoxal 5'-phosphate synthase (glutamine hydrolysing) acivicinD-erythroseD-erythronhydrazideD-erythrose 4-phosphate2-deoxy-D-ribose 5-phosphate4-phospho-D-erythronhydrazide

No evidence of orthology to BindingDB entries

Orthology Information

Ortholog Group (OrthoMCL): OG6_103407

No human ortholog(s)

Genetic Variation

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

Homozygous genotype calls only

variant type common rare doubleton singleton
synonymous 1 11 7 14
disruptive 3 13 8 27
missense 3 13 8 26

Any inclusion in genotype call

variant type common rare doubleton singleton
synonymous 2 27 6 17
disruptive 6 40 25 54
missense 6 38 22 45

PlasmoDB Total SNPs: 131

Non-coding: 113 | Synonymous: 14 | Nonsynonymous: 3 | Stop Codon: 1

Protein Information

Protein Length: 219 | Molecular Weight (kDa): 24.563

UniProt ID(s): A0A144A0A4, Q8IIK4

PDB ID(s): 2ABW, 4ADS

Isoelectric Point: 6.87

Protein Domain Annotations:

Source Family ID Description
InterPro IPR002161 Pyridoxal 5'-phosphate synthase subunit PdxT/SNO
InterPro IPR021196 PdxT/SNO family, conserved site
InterPro IPR029062 Class I glutamine amidotransferase-like
PFam PF01174 Pyridoxal 5'-phosphate synthase subunit PdxT/SNO
Superfamily SSF52317 Class I glutamine amidotransferase-like

Associated Publications

PMID Title Authors DOI/Link
12368864 Genome sequence of the human malaria parasite Plasmodium falciparum. Gardner MJ, Hall N, ..., Barrell B 10.1038/nature01097
34327152 Structural Dynamics and Perspectives of Vitamin B6 Biosynthesis Enzymes inPlasmodium: Advances and Open Questions Barra ALC, Ullah N, ..., Nascimento AS 10.3389/fcimb.2021.688380
31626961 Improved stability of polyclonal antibodies: A case study withlyophilization-conserved antibodies raised against epitopes from the malariaparasite Plasmodium falciparum Simon N, Sperber C, ..., Friedrich O 10.1016/j.ejps.2019.105086
32825141 Solution Structures and Dynamic Assembly of the 24-Meric Plasmodial Pdx1-Pdx2Complex Ullah N, Andaleeb H, ..., Wrenger C 10.3390/ijms21175971