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Q07412

- TPIS_PLAFA

UniProt

Q07412 - TPIS_PLAFA

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Protein

Triosephosphate isomerase

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

Functioni

Catalytic activityi

D-glyceraldehyde 3-phosphate = glycerone phosphate.UniRule annotation

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

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 isomeraseUniRule annotationPRO_0000090138Add
BLAST

Proteomic databases

PRIDEiQ07412.

Interactioni

Subunit structurei

Homodimer.3 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 – 106
Helixi17 – 2812
Turni34 – 363
Beta strandi37 – 426
Helixi45 – 473
Helixi48 – 547
Beta strandi59 – 646
Beta strandi71 – 733
Helixi80 – 856
Beta strandi90 – 934
Helixi96 – 1016
Helixi106 – 11813
Beta strandi122 – 1276
Helixi131 – 1355
Helixi139 – 14810
Helixi151 – 1533
Beta strandi159 – 1646
Helixi167 – 1693
Beta strandi170 – 1734
Helixi178 – 19518
Helixi198 – 2036
Beta strandi204 – 2085
Turni214 – 2163
Helixi217 – 2215
Beta strandi228 – 2314
Helixi233 – 2364
Helixi240 – 2467

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ07412.

Family & Domainsi

Sequence similaritiesi

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

MARKYFVAAN WKCNGTLESI KSLTNSFNNL DFDPSKLDVV VFPVSVHYDH    50
TRKLLQSKFS TGIQNVSKFG NGSYTGEVSA EIAKDLNIEY VIIGHFERRK 100
YFHETDEDVR EKLQASLKNN LKAVVCFGES LEQREQNKTI EVITKQVKAF 150
VDLIDNFDNV ILAYEPLWAI GTGKTATPEQ AQLVHKEIRK IVKDTCGEKQ 200
ANQIRILYGG SVNTENCSSL IQQEDIDGFL VGNASLKESF VDIIKSAM 248
Length:248
Mass (Da):27,935
Last modified:October 1, 1994 - v1
Checksum:iEFC8A4373EA9BED1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L01654 mRNA. Translation: AAA18799.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L01654 mRNA. Translation: AAA18799.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LYX X-ray 1.90 A 1-248 [» ]
1LZO X-ray 2.80 A/B/C/D 1-248 [» ]
1M7O X-ray 2.40 A/B 1-248 [» ]
1M7P X-ray 2.40 A/B 1-248 [» ]
1O5X X-ray 1.10 A/B 1-248 [» ]
1VGA X-ray 1.80 A/B/C/D 1-248 [» ]
1WOA X-ray 2.80 A/B/C/D 1-248 [» ]
1WOB X-ray 2.80 A/B/C/D 1-248 [» ]
1YDV X-ray 2.20 A/B 1-248 [» ]
2FI6 model - A 1-248 [» ]
2VFD X-ray 1.40 A/B 1-248 [» ]
2VFE X-ray 2.20 A/B 1-248 [» ]
2VFF X-ray 1.70 A/B 1-248 [» ]
2VFG X-ray 1.95 A/B/C/D 1-248 [» ]
2VFH X-ray 2.00 A/B 1-248 [» ]
2VFI X-ray 2.25 A/B 1-248 [» ]
3PSV X-ray 2.00 A/B 1-248 [» ]
3PSW X-ray 1.99 A/B 1-248 [» ]
3PVF X-ray 1.73 A 1-248 [» ]
3PWA X-ray 2.04 A/B 1-248 [» ]
3PY2 X-ray 1.93 A/B 1-248 [» ]
DisProti DP00614.
ProteinModelPortali Q07412.
SMRi Q07412. Positions 3-248.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-7137584.

Proteomic databases

PRIDEi Q07412.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0149.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00189 .
UPA00138 .

Miscellaneous databases

EvolutionaryTracei Q07412.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00147_B. TIM_B.
InterProi IPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view ]
PANTHERi PTHR21139. PTHR21139. 1 hit.
Pfami PF00121. TIM. 1 hit.
[Graphical view ]
SUPFAMi SSF51351. SSF51351. 1 hit.
TIGRFAMsi TIGR00419. tim. 1 hit.
PROSITEi PS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1993) [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(1997) [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(2002) [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(2002) [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(2003) [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(2004) [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: June 11, 2014
This is version 91 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

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