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Protein

Triosephosphate isomerase

Gene

TPI

Organism
Plasmodium falciparum
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-glyceraldehyde 3-phosphate = glycerone phosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101Substrate
Binding sitei12 – 121Substrate
Active sitei95 – 951Electrophile
Active sitei165 – 1651Proton acceptor

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. triose-phosphate isomerase activity Source: UniProtKB-EC

GO - Biological processi

  1. gluconeogenesis Source: UniProtKB-UniPathway
  2. glycolytic process Source: UniProtKB-UniPathway
  3. pentose-phosphate shunt Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Gluconeogenesis, Glycolysis, Pentose shunt

Enzyme and pathway databases

BRENDAi5.3.1.1. 4889.
UniPathwayiUPA00109; UER00189.
UPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Triosephosphate isomerase (EC:5.3.1.1)
Short name:
TIM
Alternative name(s):
Triose-phosphate isomerase
Gene namesi
Name:TPI
OrganismiPlasmodium falciparum
Taxonomic identifieri5833 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 248248Triosephosphate isomerasePRO_0000090138Add
BLAST

Proteomic databases

PRIDEiQ07412.

Interactioni

Subunit structurei

Homodimer.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-7086711,EBI-7086711

Protein-protein interaction databases

MINTiMINT-7137584.

Structurei

Secondary structure

1
248
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Helixi17 – 2812Combined sources
Turni34 – 363Combined sources
Beta strandi37 – 426Combined sources
Helixi45 – 473Combined sources
Helixi48 – 547Combined sources
Beta strandi59 – 646Combined sources
Beta strandi71 – 733Combined sources
Helixi80 – 856Combined sources
Beta strandi90 – 934Combined sources
Helixi96 – 1016Combined sources
Helixi106 – 11813Combined sources
Beta strandi122 – 1276Combined sources
Helixi131 – 1355Combined sources
Helixi139 – 14810Combined sources
Helixi151 – 1533Combined sources
Beta strandi159 – 1646Combined sources
Helixi167 – 1693Combined sources
Beta strandi170 – 1734Combined sources
Helixi178 – 19518Combined sources
Helixi198 – 2036Combined sources
Beta strandi204 – 2085Combined sources
Turni214 – 2163Combined sources
Helixi217 – 2215Combined sources
Beta strandi228 – 2314Combined sources
Helixi233 – 2364Combined sources
Helixi240 – 2467Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LYXX-ray1.90A1-248[»]
1LZOX-ray2.80A/B/C/D1-248[»]
1M7OX-ray2.40A/B1-248[»]
1M7PX-ray2.40A/B1-248[»]
1O5XX-ray1.10A/B1-248[»]
1VGAX-ray1.80A/B/C/D1-248[»]
1WOAX-ray2.80A/B/C/D1-248[»]
1WOBX-ray2.80A/B/C/D1-248[»]
1YDVX-ray2.20A/B1-248[»]
2FI6model-A1-248[»]
2VFDX-ray1.40A/B1-248[»]
2VFEX-ray2.20A/B1-248[»]
2VFFX-ray1.70A/B1-248[»]
2VFGX-ray1.95A/B/C/D1-248[»]
2VFHX-ray2.00A/B1-248[»]
2VFIX-ray2.25A/B1-248[»]
3PSVX-ray2.00A/B1-248[»]
3PSWX-ray1.99A/B1-248[»]
3PVFX-ray1.73A1-248[»]
3PWAX-ray2.04A/B1-248[»]
3PY2X-ray1.93A/B1-248[»]
DisProtiDP00614.
ProteinModelPortaliQ07412.
SMRiQ07412. Positions 3-248.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07412.

Family & Domainsi

Sequence similaritiesi

Belongs to the triosephosphate isomerase family.Curated

Phylogenomic databases

eggNOGiCOG0149.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00147_B. TIM_B.
InterProiIPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]
PANTHERiPTHR21139. PTHR21139. 1 hit.
PfamiPF00121. TIM. 1 hit.
[Graphical view]
SUPFAMiSSF51351. SSF51351. 1 hit.
TIGRFAMsiTIGR00419. tim. 1 hit.
PROSITEiPS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q07412-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARKYFVAAN WKCNGTLESI KSLTNSFNNL DFDPSKLDVV VFPVSVHYDH
60 70 80 90 100
TRKLLQSKFS TGIQNVSKFG NGSYTGEVSA EIAKDLNIEY VIIGHFERRK
110 120 130 140 150
YFHETDEDVR EKLQASLKNN LKAVVCFGES LEQREQNKTI EVITKQVKAF
160 170 180 190 200
VDLIDNFDNV ILAYEPLWAI GTGKTATPEQ AQLVHKEIRK IVKDTCGEKQ
210 220 230 240
ANQIRILYGG SVNTENCSSL IQQEDIDGFL VGNASLKESF VDIIKSAM
Length:248
Mass (Da):27,935
Last modified:October 1, 1994 - v1
Checksum:iEFC8A4373EA9BED1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01654 mRNA. Translation: AAA18799.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01654 mRNA. Translation: AAA18799.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LYXX-ray1.90A1-248[»]
1LZOX-ray2.80A/B/C/D1-248[»]
1M7OX-ray2.40A/B1-248[»]
1M7PX-ray2.40A/B1-248[»]
1O5XX-ray1.10A/B1-248[»]
1VGAX-ray1.80A/B/C/D1-248[»]
1WOAX-ray2.80A/B/C/D1-248[»]
1WOBX-ray2.80A/B/C/D1-248[»]
1YDVX-ray2.20A/B1-248[»]
2FI6model-A1-248[»]
2VFDX-ray1.40A/B1-248[»]
2VFEX-ray2.20A/B1-248[»]
2VFFX-ray1.70A/B1-248[»]
2VFGX-ray1.95A/B/C/D1-248[»]
2VFHX-ray2.00A/B1-248[»]
2VFIX-ray2.25A/B1-248[»]
3PSVX-ray2.00A/B1-248[»]
3PSWX-ray1.99A/B1-248[»]
3PVFX-ray1.73A1-248[»]
3PWAX-ray2.04A/B1-248[»]
3PY2X-ray1.93A/B1-248[»]
DisProtiDP00614.
ProteinModelPortaliQ07412.
SMRiQ07412. Positions 3-248.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-7137584.

Proteomic databases

PRIDEiQ07412.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG0149.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00189.
UPA00138.
BRENDAi5.3.1.1. 4889.

Miscellaneous databases

EvolutionaryTraceiQ07412.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00147_B. TIM_B.
InterProiIPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]
PANTHERiPTHR21139. PTHR21139. 1 hit.
PfamiPF00121. TIM. 1 hit.
[Graphical view]
SUPFAMiSSF51351. SSF51351. 1 hit.
TIGRFAMsiTIGR00419. tim. 1 hit.
PROSITEiPS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning of the triosephosphate isomerase gene of Plasmodium falciparum and expression in Escherichia coli."
    Ranie J., Kumar V.P., Balaram H.
    Mol. Biochem. Parasitol. 61:159-169(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Palo Alto.
  2. "Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design."
    Velanker S.S., Ray S.S., Gokhale R.S., Suma S., Balaram H., Balaram P., Murthy M.R.N.
    Structure 5:751-761(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), HOMODIMERIZATION.
  3. "Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: observation of the catalytic loop in the open conformation in the ligand-bound state."
    Parthasarathy S., Balaram H., Balaram P., Murthy M.R.N.
    Acta Crystallogr. D 58:1992-2000(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, HOMODIMERIZATION.
  4. "Structure of the Plasmodium falciparum triosephosphate isomerase-phosphoglycolate complex in two crystal forms: characterization of catalytic loop open and closed conformations in the ligand-bound state."
    Parthasarathy S., Ravindra G., Balaram H., Balaram P., Murthy M.R.N.
    Biochemistry 41:13178-13188(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, HOMODIMERIZATION.
  5. "Structure of Plasmodium falciparum triose-phosphate isomerase-2-phosphoglycerate complex at 1.1-A resolution."
    Parthasarathy S., Eaazhisai K., Balaram H., Balaram P., Murthy M.R.N.
    J. Biol. Chem. 278:52461-52470(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
  6. "Structures of unliganded and inhibitor complexes of W168F, a Loop6 hinge mutant of Plasmodium falciparum triosephosphate isomerase: observation of an intermediate position of loop6."
    Eaazhisai K., Balaram H., Balaram P., Murthy M.R.N.
    J. Mol. Biol. 343:671-684(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.

Entry informationi

Entry nameiTPIS_PLAFA
AccessioniPrimary (citable) accession number: Q07412
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 1, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.