Reviewed, UniProtKB/Swiss-Prot P04789 (TPIS_TRYBB)

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 brucei brucei
Taxonomic identifier	5702 [NCBI]
Taxonomic lineage	Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma

Protein attributes

Sequence length	250 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.3 Ref.4
Subcellular location	Glycosome.
Miscellaneous	The enzyme contains a high proportion of positively-charged residues in beta-barrels V and VII (compared to the homologous regions in other triose isomerase sequences). Since 2 clusters of positive charges located at precise distances on the molecular surface are common to 4 glycosomal enzymes, it has been speculated that this might represent a signal for entry into glycosomes (Ref.1).
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 Direct protein sequencing
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 – 250

250

Triosephosphate isomerase, glycosomal

PRO_0000090142

Sites

Active site

95

1

Electrophile

Active site

167

1

Proton acceptor

Binding site

11

1

Substrate

Binding site

13

1

Substrate

Secondary structure

1

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250

Helix Strand Turn

Details...

Beta strand

7 – 11

5

Helix

18 – 29

12

Beta strand

38 – 42

5

Helix

45 – 47

3

Helix

48 – 54

7

Beta strand

60 – 65

6

Beta strand

68 – 70

3

Helix

80 – 85

6

Beta strand

90 – 94

5

Helix

96 – 101

6

Helix

106 – 119

14

Beta strand

122 – 127

6

Helix

131 – 135

5

Helix

139 – 152

14

Helix

156 – 161

6

Beta strand

162 – 167

6

Helix

169 – 171

3

Helix

180 – 197

18

Helix

200 – 205

6

Beta strand

208 – 213

6

Turn

216 – 218

3

Helix

219 – 223

5

Beta strand

230 – 234

5

Helix

235 – 238

4

Helix

242 – 247

6

Sequences

	Sequence		Length	Mass (Da)
	P04789-1 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: 189D7A00632040FE	FASTA	250	26,835
	10 20 30 40 50 60 MSKPQPIAAA NWKCNGSQQS LSELIDLFNS TSINHDVQCV VASTFVHLAM TKERLSHPKF 70 80 90 100 110 120 VIAAQNAIAK SGAFTGEVSL PILKDFGVNW IVLGHSERRA YYGETNEIVA DKVAAAVASG 130 140 150 160 170 180 FMVIACIGET LQERESGRTA VVVLTQIAAI AKKLKKADWA KVVIAYEPVW AIGTGKVATP 190 200 210 220 230 240 QQAQEAHALI RSWVSSKIGA DVAGELRILY GGSVNGKNAR TLYQQRDVNG FLVGGASLKP 250 EFVDIIKATQ

References

[1]	"Characterization of the gene for the microbody (glycosomal) triosephosphate isomerase of Trypanosoma brucei." Swinkels B.W., Gibson W.C., Osinga K.A., Kramer R., Veeneman G.H., van Boom J.H., Borst P. EMBO J. 5:1291-1298(1986) [PubMed: 3015595] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"How proteins get into microbodies (peroxisomes, glyoxysomes, glycosomes)." Borst P. Biochim. Biophys. Acta 866:179-203(1986) [PubMed: 3516224] [Abstract] Cited for: PROTEIN SEQUENCE.
[3]	"Structure determination of the glycosomal triosephosphate isomerase from Trypanosoma brucei brucei at 2.4-A resolution." Wierenga R.K., Kalk K.H., Hol W.G.J. J. Mol. Biol. 198:109-121(1987) [PubMed: 3430602] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), HOMODIMERIZATION.
[4]	"Refined 1.83 A structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3-phosphate complex." Wierenga R.K., Noble M.E.M., Vriend G., Nauche S., Hol W.G.J. J. Mol. Biol. 220:995-1015(1991) [PubMed: 1880808] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS), HOMODIMERIZATION.
[5]	"The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes." Noble M.E., Wierenga R.K., Lambeir A.-M., Opperdoes F.R., Thunnissen A.M., Kalk K.H., Groendijk H., Hol W.G.J. Proteins 10:50-69(1991) [PubMed: 2062828] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
[6]	"Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase." Wierenga R.K., Noble M.E.M., Davenport R.C. J. Mol. Biol. 224:1115-1126(1992) [PubMed: 1569570] [Abstract] Cited for: COMPARISON OF X-RAY STRUCTURES.
[7]	"Overexpression of trypanosomal triosephosphate isomerase in Escherichia coli and characterisation of a dimer-interface mutant." Borchert T.V., Pratt K., Zeelen J.P., Callens M., Noble M.E.M., Opperdoes F.R., Michels P.A.M., Wierenga R.K. Eur. J. Biochem. 211:703-710(1993) [PubMed: 8436128] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), SEQUENCE REVISION TO 203.
[8]	"Three new crystal structures of point mutation variants of monoTIM: conformational flexibility of loop-1, loop-4 and loop-8." Borchert T.V., Kishan K.V., Zeelen J.P., Schliebs W., Thanki N., Abagyan R., Jaenicke R., Wierenga R.K. Structure 3:669-679(1995) [PubMed: 8591044] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANTS IN COMPLEX WITH SUBSTRATE ANALOGS.
[9]	"The importance of the conserved Arg191-Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis." Kursula I., Partanen S., Lambeir A.-M., Wierenga R.K. FEBS Lett. 518:39-42(2002) [PubMed: 11997014] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X03921 Genomic DNA. Translation: CAA27559.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AG1	X-ray	2.36	O/T	1-250	[»]
1DKW	X-ray	2.65	A/B	2-250	[»]
1IIG	X-ray	2.60	A/B	1-250	[»]
1IIH	X-ray	2.20	A/B	1-250	[»]
1KV5	X-ray	1.65	A/B	1-250	[»]
1ML1	X-ray	2.60	A/C/E/G/I/K	1-250	[»]
1MSS	X-ray	2.40	A/B	1-250	[»]
1MTM	model	-	A	1-250	[»]
1TPD	X-ray	2.10	A/B	1-250	[»]
1TPE	X-ray	2.10	A	1-250	[»]
1TPF	X-ray	1.80	A/B	1-250	[»]
1TRD	X-ray	2.50	A/B	1-250	[»]
1TRI	X-ray	2.40	A	1-250	[»]
1TSI	X-ray	2.84	A/B	1-250	[»]
1TTI	X-ray	2.40	A	1-250	[»]
1TTJ	X-ray	2.40	A	1-250	[»]
2J24	X-ray	2.10	A/B	1-250	[»]
2J27	X-ray	1.15	A/B	1-250	[»]
2V0T	X-ray	2.20	A/B/C/D/E/F/G/H	1-250	[»]
2V2C	X-ray	1.89	A	1-250	[»]
2V2D	X-ray	2.30	A	1-250	[»]
2V2H	X-ray	1.18	A/B/C	1-250	[»]
2V5L	X-ray	2.40	A/B	1-250	[»]
2VEI	X-ray	1.89	A/B/C	2-250	[»]
2VEK	X-ray	1.60	A/B	2-250	[»]
2VEL	X-ray	2.30	A/B	2-250	[»]
2VEM	X-ray	2.20	A/B	2-250	[»]
2VEN	X-ray	2.00	A/B	2-250	[»]
2WSQ	X-ray	2.10	A/B/C/D	2-250	[»]
2WSR	X-ray	1.65	A	2-250	[»]
3TIM	X-ray	2.80	A/B	1-250	[»]
4TIM	X-ray	2.40	A/B	1-250	[»]
5TIM	X-ray	1.83	A/B	1-250	[»]
6TIM	X-ray	2.20	A/B	1-250	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

5.3.1.1. 74165.

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...

Other Resources

DrugBank

DB01093. Dimethyl sulfoxide.

Entry information

Entry name

TPIS_TRYBB

Accession

Primary (citable) accession number: P04789

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	February 1, 1995
Last modified:	November 24, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)