About Gene List

PF3D7_1206400 (TUM1)

Genome location: Pf3D7_12_v3:290,276..291,876(+)

Genome classification: Core

Function and Localization

Product Description: thiosulfate sulfurtransferase, putative

SignalP Peptide: N/A

# Transmembrane Domains: 0

EC Numbers: 2.8.1.1 (Thiosulfate sulfurtransferase)

Curated GO (PlasmoDB):

Type GO Term Name
Component GO:0005739 mitochondrion
Function GO:0004792 thiosulfate sulfurtransferase activity
Process GO:0002098 tRNA wobble uridine modification
Process GO:0019346 transsulfuration

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 0.01 1.00
Trophozoite not expressed 0.03 0.98
Schizont possibly expressed 0.19 0.87
Gametocyte not expressed 0.07 0.96

More info:

Resistome Mutations

Old (Pf3D7v3) Gene ID: PF3D7_1206400

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: Mutable in CDS

MIS: 0.999 | MFS: -0.46 | #Insertions: 2

PlasmoGEM Phenotype: N/A

RMgmDB ABS Phenotype: N/A

More info: PhenoPlasm Link

Binding Evidence

AlphaFill Uniprot ID: Q8I5Y1

"Best" AlphaFill ligand hit: PYR (pyruvic acid, Local RMSD=4.65) with 4JGT (Global RMSD=4.39)

BRENDA EC Inhibitors:

EC # Name EC Inhibitors
2.8.1.1 thiosulfate sulfurtransferase NEMSDSH2SCaCl2SO42-SO32-malateanionssulfitecitrateSulfidelipoate...

Orthology to BindingDB Entries:

UniProt Protein Name Species Homology Source BindingDB Ligands
Q16762 Thiosulfate sulfurtransferase OrthoDB Beta lapachoneHARMALOLmethylthioninium chlorideRiboflavin sodium phosphate...

Orthology Information

Ortholog Group (OrthoMCL): OG6_150855

No human ortholog(s)

Protein Information

Protein Length: 346 | Molecular Weight (kDa): 41.929

UniProt ID(s): Q8I5Y1

PDB ID(s): None

Isoelectric Point: 7.23

Protein Domain Annotations:

Source Family ID Description
InterPro IPR001763 Rhodanese-like domain
InterPro IPR036873 Rhodanese-like domain superfamily
PFam PF00581 Rhodanese-like domain
Superfamily SSF52821 Rhodanese-like domain superfamily

Genetic Variation

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

Homozygous genotype calls only

variant type common rare doubleton singleton
synonymous 1 16 4 21
disruptive 1 26 21 71
missense 1 25 20 63

Any inclusion in genotype call

variant type common rare doubleton singleton
synonymous 1 34 10 25
disruptive 9 71 35 90
missense 5 59 28 68

PlasmoDB Total SNPs: 55

Non-coding: 47 | Synonymous: 6 | Nonsynonymous: 2 | 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
21821903 Crystallization and preliminary X-ray analysis of the yeast tRNA-thiouridinemodification protein 1 (Tum1p) Qiu R, Wang F, ..., Ji C 10.1107/S1744309111024900
28357324 Sulfur transfer and activation by ubiquitin-like modifier system Uba4*Urm1 linkprotein urmylation and tRNA thiolation in yeast Judes A, Bruch A, ..., Schaffrath R 10.15698/mic2016.11.539
31240288 Iterative synthetic strategies and gene deletant experiments enable the firstidentification of polysulfides in Saccharomyces cerevisiae Pilkington LI, Deed RC, ..., Fedrizzi B 10.1039/c9cc03020d
22587783 Crystal structure of the Tum1 protein from the yeast Saccharomyces cerevisiae Qiu R, Wang F, ..., Ji C 10.2174/092986612803217060
27915245 The yeast TUM1 affects production of hydrogen sulfide from cysteine treatmentduring fermentation Huang CW, Walker ME, ..., Jiranek V 10.1093/femsyr/fow100
28830344 Tum1 is involved in the metabolism of sterol esters in Saccharomyces cerevisiae Ursic K, Ogrizovic M, ..., Petrovic U 10.1186/s12866-017-1088-1
33001274 Identification and characterization of a sulfite reductase gene and new insightsregarding the sulfur-containing amino acid metabolism in the basidiomycetousyeast Cryptococcus neoformans Nguyen PT, Toh-E A, ..., Shimizu K 10.1007/s00294-020-01112-9