About Gene List

PF3D7_1405600 (RNR)

Genome location: Pf3D7_14_v3:192,727..194,345(-)

Genome classification: Core

Function and Localization

Product Description: ribonucleoside-diphosphate reductase small chain, putative

SignalP Peptide: N/A

# Transmembrane Domains: 0

EC Numbers: 1.17.4.1 (Ribonucleoside-diphosphate reductase)

Curated GO (PlasmoDB):

Type GO Term Name
Component GO:0005622 intracellular
Component GO:0005971 ribonucleoside-diphosphate reductase complex
Function GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
Process GO:0009263 deoxyribonucleotide biosynthetic process

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 0.04 0.98
Trophozoite expressed 0.35 0.78
Schizont expressed 0.16 0.89
Gametocyte expressed 0.26 0.84

More info:

Resistome Mutations

Old (Pf3D7v3) Gene ID: PF3D7_1405600

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: 0.12 | MFS: -2.846 | #Insertions: 0

PlasmoGEM Phenotype: Essential (Pb ortholog: PBANKA_1036600)

  • Relative Growth Rate: 0.15 ± 0.47
  • Confidence: 2.89

RMgmDB ABS Phenotype: Different from wild type (Pb ortholog: PY17X_1039000)

Modification: Tagged | RMgm-1555

More info: PhenoPlasm Link

Binding Evidence

AlphaFill Uniprot ID: Q8IM38

"Best" AlphaFill ligand hit: FMN (flavin mononucleotide, Local RMSD=5.46) with 4BMO (Global RMSD=4.73)

BRENDA EC Inhibitors:

EC # Name EC Inhibitors
1.17.4.1 ribonucleoside-diphosphate reductase BRENDA SOAP query unsuccessful

Orthology to BindingDB Entries:

UniProt Protein Name Species Homology Source BindingDB Ligands
P31350 Ribonucleoside-diphosphate reductase subunit M2 Homo sapiens OMA, OrthoDB CHEMBL420050CHEMBL314693CHEMBL86963CHEMBL313203...

Orthology Information

Ortholog Group (OrthoMCL): OG6_100537

Most Similar Human Ortholog: P31350

TM-align score: 0.89 | RMSD: 2.01

Seq Identity: 0.57 | Length: 325 / 349

All Human Orthologs (OrthoMCL):

Gene ID Description
ENSG00000048392 ribonucleotide reductase regulatory TP53 inducible subunit M2B
ENSG00000171848 ribonucleotide reductase regulatory subunit M2

Protein Information

Protein Length: 349 | Molecular Weight (kDa): 40.6

UniProt ID(s): Q8IM38, Q9U428

PDB ID(s): None

Isoelectric Point: 5.2

Protein Domain Annotations:

Source Family ID Description
InterPro IPR000358 Ribonucleotide reductase small subunit family
InterPro IPR009078 Ferritin-like superfamily
InterPro IPR030475 Ribonucleotide reductase small subunit, acitve site
InterPro IPR033909 Ribonucleotide reductase small subunit
PFam PF00268 Ribonucleotide reductase small subunit family
Superfamily SSF47240 Ferritin-like superfamily

Genetic Variation

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

Homozygous genotype calls only

variant type common rare doubleton singleton
synonymous 3 26 16 29
disruptive 0 5 3 14
missense 0 5 3 14

Any inclusion in genotype call

variant type common rare doubleton singleton
synonymous 5 55 20 27
disruptive 1 19 29 62
missense 1 12 26 50

PlasmoDB Total SNPs: 80

Non-coding: 68 | Synonymous: 9 | Nonsynonymous: 3 | Stop Codon: 0

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
15769467 Two Plasmodium falciparum ribonucleotide reductase small subunits, PfR2 and PfR4,interact with each other and are components of the in vivo enzyme complex. Bracchi-Ricard V, Moe D, Chakrabarti D 10.1016/j.jmb.2005.01.051
27503796 Proteome mapping of Plasmodium: identification of the P. yoelii remodellome. Siau A, Huang X, ..., Preiser PR 10.1038/srep31055
38188419 A missense mutation in the suc22 gene encoding the small subunit ofribonucleotide reductase significantly sensitizes fission yeast to chronictreatment with hydroxyurea Davi K, Yurtsever I, Xu YJ 10.17912/micropub.biology.001041