Q07412 (TPIS_PLAFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Triosephosphate isomerase
Short name=TIM
EC=5.3.1.1

Alternative name(s):
Triose-phosphate isomerase

Gene names

Name:

TPI

Organism

Plasmodium falciparum

Taxonomic identifier

5833 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Laverania)

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	D-glyceraldehyde 3-phosphate = glycerone phosphate.
Pathway	Carbohydrate biosynthesis; gluconeogenesis. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1.
Subunit structure	Homodimer. Ref.2 Ref.3 Ref.4
Sequence similarities	Belongs to the triosephosphate isomerase family.

Ontologies

Keywords
Biological process	Gluconeogenesis Glycolysis Pentose shunt
Molecular function	Isomerase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-UniPathway glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway pentose-phosphate shunt Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	triose-phosphate isomerase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 248

248

Triosephosphate isomerase

PRO_0000090138

Sites

Active site

95

1

Electrophile

Active site

165

1

Proton acceptor

Binding site

10

1

Substrate

Binding site

12

1

Substrate

Secondary structure

1

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248

Helix Strand Turn

Details...

Beta strand

5 – 10

6

Helix

17 – 28

12

Turn

34 – 36

3

Beta strand

37 – 42

6

Helix

45 – 47

3

Helix

48 – 54

7

Beta strand

59 – 64

6

Beta strand

71 – 73

3

Helix

80 – 85

6

Beta strand

90 – 93

4

Helix

96 – 101

6

Helix

106 – 118

13

Beta strand

122 – 127

6

Helix

131 – 135

5

Helix

139 – 148

10

Helix

151 – 153

3

Beta strand

159 – 164

6

Helix

167 – 169

3

Beta strand

170 – 173

4

Helix

178 – 195

18

Helix

198 – 203

6

Beta strand

204 – 208

5

Turn

214 – 216

3

Helix

217 – 221

5

Beta strand

228 – 231

4

Helix

233 – 236

4

Helix

240 – 246

7

Sequences

	Sequence		Length	Mass (Da)
	Q07412 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: EFC8A4373EA9BED1	FASTA	248	27,935
	10 20 30 40 50 60 MARKYFVAAN WKCNGTLESI KSLTNSFNNL DFDPSKLDVV VFPVSVHYDH TRKLLQSKFS 70 80 90 100 110 120 TGIQNVSKFG NGSYTGEVSA EIAKDLNIEY VIIGHFERRK YFHETDEDVR EKLQASLKNN 130 140 150 160 170 180 LKAVVCFGES LEQREQNKTI EVITKQVKAF VDLIDNFDNV ILAYEPLWAI GTGKTATPEQ 190 200 210 220 230 240 AQLVHKEIRK IVKDTCGEKQ ANQIRILYGG SVNTENCSSL IQQEDIDGFL VGNASLKESF VDIIKSAM

References

[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L01654 mRNA. Translation: AAA18799.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q07412.

SMR

Q07412. Positions 3-248.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-7137584.

Proteomic databases

PRIDE

Q07412.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

eggNOG

COG0149.

Enzyme and pathway databases

UniPathway

UPA00109; UER00189.
UPA00138.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]

PANTHER

PTHR21139. PTHR21139. 1 hit.

Pfam

PF00121. TIM. 1 hit.
[Graphical view]

SUPFAM

SSF51351. Triophos_ismrse. 1 hit.

TIGRFAMs

TIGR00419. tim. 1 hit.

PROSITE

PS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q07412.

Entry information

Entry name

TPIS_PLAFA

Accession

Primary (citable) accession number: Q07412

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)