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PLAFA:TPIS
Contents
| Species (Taxon ID) | Plasmodium falciparum. (5833) | |
| Gene Name(s) | TPI | |
| Protein Name(s) | Triosephosphate isomerase
TIM Triose-phosphate isomerase | |
| External Links | ||
| UniProt | Q07412 | |
| EMBL | L01654 | |
| PDB | 1LYX 1LZO 1M7O 1M7P 1O5X 1VGA 1WOA 1WOB 1YDV 2FI6 2VFD 2VFE 2VFF 2VFG 2VFH 2VFI 3PSV 3PSW 3PVF 3PWA 3PY2 | |
| PDBsum | 1LYX 1LZO 1M7O 1M7P 1O5X 1VGA 1WOA 1WOB 1YDV 2FI6 2VFD 2VFE 2VFF 2VFG 2VFH 2VFI 3PSV 3PSW 3PVF 3PWA 3PY2 | |
| DisProt | DP00614 | |
| ProteinModelPortal | Q07412 | |
| SMR | Q07412 | |
| MINT | MINT-7137584 | |
| PRIDE | Q07412 | |
| eggNOG | COG0149 | |
| UniPathway | UPA00109 UPA00138 | |
| EvolutionaryTrace | Q07412 | |
| GO | GO:0042802 GO:0004807 GO:0006094 GO:0006096 GO:0006098 | |
| Gene3D | 3.20.20.70 | |
| HAMAP | MF_00147_B | |
| InterPro | IPR013785 IPR022896 IPR000652 IPR020861 | |
| PANTHER | PTHR21139 | |
| Pfam | PF00121 | |
| SUPFAM | SSF51351 | |
| TIGRFAMs | TIGR00419 | |
| PROSITE | PS00171 PS51440 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0004807 |
triose-phosphate isomerase activity |
ECO:0000314 |
F |
Figure 6 shows that the recombinant TPI enzymes are able to convert glyceraldehyde-3-phosphate to dihydroxyacetone phosphate at a much greater rate than the controls. |
complete | |||||
|
enables |
GO:0004807 |
triose-phosphate isomerase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0003824 |
catalytic activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004807 |
triose-phosphate isomerase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR000652 |
F |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0006096 |
glycolytic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004807 |
triose-phosphate isomerase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006096 |
glycolytic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0324 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0016853 |
isomerase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006094 |
gluconeogenesis |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0312 |
P |
Seeded From UniProt |
complete | ||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Ranie, J et al. (1993) Cloning of the triosephosphate isomerase gene of Plasmodium falciparum and expression in Escherichia coli. Mol. Biochem. Parasitol. 61 159-69 PubMed GONUTS page
- ↑ Samanta, M et al. (2011) Probing the role of the fully conserved Cys126 in triosephosphate isomerase by site-specific mutagenesis--distal effects on dimer stability. FEBS J. 278 1932-43 PubMed GONUTS page
- ↑ Banerjee, M et al. (2009) Structural effects of a dimer interface mutation on catalytic activity of triosephosphate isomerase. The role of conserved residues and complementary mutations. FEBS J. 276 4169-83 PubMed GONUTS page
