Reviewed, UniProtKB/Swiss-Prot P52270 (TPIS_TRYCR)

Names and origin

Protein names	Recommended name:     Triosephosphate isomerase, glycosomal       Short name=TIM       Short name=Triose-phosphate isomerase     EC=5.3.1.1
Organism	Trypanosoma cruzi
Taxonomic identifier	5693 [NCBI]
Taxonomic lineage	Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma › Schizotrypanum

Protein attributes

Sequence length	251 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
Subcellular location	Glycosome.
Sequence similarities	Belongs to the triosephosphate isomerase family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Gluconeogenesis Glycolysis Lipid synthesis Pentose shunt
Cellular component	Glycosome Peroxisome
Molecular function	Isomerase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-KW glycolysis Inferred from electronic annotation. Source: UniProtKB-KW pentose-phosphate shunt Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	glycosome Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 251

251

Triosephosphate isomerase, glycosomal

PRO_0000090143

Sites

Active site

96

1

Electrophile By similarity

Active site

168

1

Proton acceptor By similarity

Binding site

12

1

Substrate By similarity

Binding site

14

1

Substrate By similarity

Secondary structure

1

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251

Helix Strand Turn

Details...

Beta strand

8 – 12

5

Helix

19 – 31

13

Beta strand

39 – 43

5

Helix

46 – 48

3

Helix

49 – 55

7

Beta strand

61 – 66

6

Beta strand

69 – 71

3

Helix

81 – 86

6

Beta strand

91 – 94

4

Helix

97 – 102

6

Helix

107 – 120

14

Beta strand

123 – 128

6

Helix

132 – 136

5

Helix

140 – 152

13

Helix

157 – 162

6

Beta strand

163 – 167

5

Helix

170 – 172

3

Beta strand

173 – 176

4

Helix

181 – 199

19

Helix

201 – 206

6

Beta strand

208 – 214

7

Turn

217 – 219

3

Helix

220 – 224

5

Beta strand

231 – 235

5

Helix

236 – 239

4

Helix

242 – 248

7

Sequences

	Sequence		Length	Mass (Da)
	P52270-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 03010B66586C186D	FASTA	251	27,329
	10 20 30 40 50 60 MASKPQPIAA ANWKCNGSES LLVPLIETLN AATFDHDVQC VVAPTFLHIP MTKARLTNPK 70 80 90 100 110 120 FQIAAQNAIT RSGAFTGEVS LQILKDYGIS WVVLGHSERR LYYGETNEIV AEKVAQACAA 130 140 150 160 170 180 GFHVIVCVGE TNEEREAGRT AAVVLTQLAA VAQKLSKEAW SRVVIAYEPV WAIGTGKVAT 190 200 210 220 230 240 PQQAQEVHEL LRRWVRSKLG TDIAAQLRIL YGGSVTAKNA RTLYQMRDIN GFLVGGASLK 250 PEFVEIIEAT K

References

[1]	"Cloning, expression, purification and characterization of triosephosphate isomerase from Trypanosoma cruzi." Ostoa-Saloma P., Garza-Ramos G., Ramirez J., Becker I., Berzunza M., Landa A., Gomez-Puyou A., Tuena de Gomez-Puyou M., Perez-Montfort R. Eur. J. Biochem. 244:700-705(1997) [PubMed: 9108237] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Ninoa.
[2]	"Differences in the intersubunit contacts in triosephosphate isomerase from two closely related pathogenic trypanosomes." Maldonado E., Soriano-Garcia M., Moreno A., Cabrera N., Garza-Ramos G., Tuena de Gomez-Puyou M., Gomez-Puyou A., Perez-Montfort R. J. Mol. Biol. 283:193-203(1998) [PubMed: 9761683] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS), HOMODIMERIZATION. Strain: Ninoa.
[3]	"Crystal structure of triosephosphate isomerase from Trypanosoma cruzi in hexane." Gao X.-G., Maldonado E., Perez-Montfort R., Garza-Ramos G., Tuena de Gomez-Puyou M., Gomez-Puyou A., Rodriguez-Romero A. Proc. Natl. Acad. Sci. U.S.A. 96:10062-10067(1999) [PubMed: 10468562] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), HOMODIMERIZATION. Strain: Ninoa.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U53867 Genomic DNA. Translation: AAB58349.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CI1	X-ray	2.00	A/B	1-251	[»]
1SUX	X-ray	2.00	A/B	1-251	[»]
1TCD	X-ray	1.83	A/B	3-251	[»]
2OMA	X-ray	2.15	A/B	2-251	[»]
2V5B	X-ray	2.00	A	1-251	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

5.3.1.1. 884.

Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

PANTHER

PTHR21139. Triophos_ismrse. 1 hit.

Pfam

PF00121. TIM. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00419. tim. 1 hit.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

TPIS_TRYCR

Accession

Primary (citable) accession number: P52270

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 24, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)