Product Description: lipoate-protein ligase 1
SignalP Peptide: N/A
# Transmembrane Domains: 0
EC Numbers: 2.3.1.181 (Lipoyl(octanoyl) transferase);2.7.7.63 (Transferred entry: 6.3.1.20);6.3.1.20 (Lipoate--protein ligase)
Curated GO (PlasmoDB):
| Type | GO Term | Name |
|---|---|---|
| Component | GO:0005737 | cytoplasm |
| Component | GO:0005739 | mitochondrion |
| Function | GO:0016979 | lipoate-protein ligase activity |
| Function | GO:0017118 | lipoyltransferase activity |
| Process | GO:0006629 | lipid metabolic process |
| Process | GO:0009249 | protein lipoylation |
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 | expressed | 0.08 | 0.96 |
| Trophozoite | expressed | 0.26 | 0.84 |
| Schizont | possibly expressed | 0.04 | 0.97 |
| Gametocyte | not expressed | 0.11 | 0.93 |
More info:
Old (Pf3D7v3) Gene ID: PF3D7_1314600
Resistome Missense Mutations: None
Resistome Compounds with Missense Mutations: None
Resistome # Samples with Disruptive Mutations: 0 (0 missense, 0 "interesting" missense)
Zhang Phenotype: Non - Mutable in CDS
MIS: 0.539 | MFS: -3.461 | #Insertions: 0
PlasmoGEM Phenotype: Essential (Pb ortholog: PBANKA_1413100)
RMgmDB ABS Phenotype: N/A
More info: PhenoPlasm Link
AlphaFill Uniprot ID: Q8IEG9
"Best" AlphaFill ligand hit: LPA (lipoic acid, Local RMSD=0.08) with 5T8U (Global RMSD=0.71)
BRENDA EC Inhibitors:
No evidence of orthology to BindingDB entries
Ortholog Group (OrthoMCL): OG6_101366
Most Similar Human Ortholog: C9JUU5
TM-align score: 0.80 | RMSD: 2.34
Seq Identity: 0.32 | Length: 219 / 408
All Human Orthologs (OrthoMCL):
| Gene ID | Description |
|---|---|
| ENSG00000144182 | lipoyltransferase 1 |
MalariaGEN Pf7 (worldwide samples) # unique SNV/indels:
Homozygous genotype calls only
| variant type | common | rare | doubleton | singleton |
|---|---|---|---|---|
| synonymous | 5 | 18 | 7 | 22 |
| disruptive | 5 | 15 | 18 | 43 |
| missense | 5 | 15 | 17 | 40 |
Any inclusion in genotype call
| variant type | common | rare | doubleton | singleton |
|---|---|---|---|---|
| synonymous | 10 | 27 | 19 | 18 |
| disruptive | 10 | 53 | 40 | 61 |
| missense | 9 | 41 | 30 | 47 |
PlasmoDB Total SNPs: 46
Non-coding: 23 | Synonymous: 19 | Nonsynonymous: 4 | Stop Codon: 0
Protein Length: 408 | Molecular Weight (kDa): 47.943
UniProt ID(s): Q8IEG9
PDB ID(s): 5T8U
Isoelectric Point: 9.05
Protein Domain Annotations:
| Source | Family ID | Description |
|---|---|---|
| InterPro | IPR004143 | Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain |
| InterPro | IPR004562 | Lipoyltransferase/lipoate-protein ligase |
| InterPro | IPR019491 | Lipoate protein ligase, C-terminal |
| PFam | PF03099 | Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain |
| PFam | PF10437 | Lipoate protein ligase, C-terminal |
| Superfamily | SSF55681 | N/A |
| Superfamily | SSF82649 |
| PMID | Title | Authors | DOI/Link |
|---|---|---|---|
| 15225307 | The human malaria parasite Plasmodium falciparum has distinct organelle-specificlipoylation pathways. | Wrenger C, Muller S | 10.1111/j.1365-2958.2004.04112.x |
| 17244193 | Scavenging of the cofactor lipoate is essential for the survival of the malariaparasite Plasmodium falciparum. | Allary M, Lu JZ, Zhu L, Prigge ST | 10.1111/j.1365-2958.2007.05592.x |
| 25116855 | Redox-dependent lipoylation of mitochondrial proteins in Plasmodium falciparum. | Afanador GA, Matthews KA, ..., Prigge ST | 10.1111/mmi.12753 |
| 34494883 | A Prioritized and Validated Resource of Mitochondrial Proteins in PlasmodiumIdentifies Unique Biology. | van Esveld SL, Meerstein-Kessel L, ..., Huynen MA | 10.1128/mSphere.00614-21 |
| 28543853 | Crystal structure of lipoate-bound lipoate ligase 1, LipL1, from Plasmodiumfalciparum | Guerra AJ, Afanador GA, Prigge ST | 10.1002/prot.25324 |