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Protein

Triosephosphate isomerase, glycosomal

Gene
N/A
Organism
Trypanosoma brucei brucei
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: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Pathwayi: glycolysis

This protein is involved in step 1 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate from glycerone phosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. Triosephosphate isomerase, glycosomal
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate from glycerone phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111Substrate
Binding sitei13 – 131Substrate
Active sitei95 – 951Electrophile
Active sitei167 – 1671Proton acceptor

GO - Molecular functioni

  • triose-phosphate isomerase activity Source: GeneDB

GO - Biological processi

  • gluconeogenesis Source: UniProtKB-UniPathway
  • glycolytic process Source: GeneDB
  • 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. 6519.
SABIO-RKP04789.
UniPathwayiUPA00109; UER00189.
UPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Triosephosphate isomerase, glycosomal (EC:5.3.1.1)
Short name:
TIM
Short name:
Triose-phosphate isomerase
OrganismiTrypanosoma brucei brucei
Taxonomic identifieri5702 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Subcellular locationi

GO - Cellular componenti

  • glycosome Source: GeneDB
Complete GO annotation...

Keywords - Cellular componenti

Glycosome, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 250250Triosephosphate isomerase, glycosomalPRO_0000090142Add
BLAST

Proteomic databases

PRIDEiP04789.

Interactioni

Subunit structurei

Homodimer.3 Publications

Structurei

Secondary structure

1
250
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115Combined sources
Beta strandi14 – 163Combined sources
Helixi18 – 2912Combined sources
Beta strandi38 – 425Combined sources
Helixi45 – 473Combined sources
Helixi48 – 547Combined sources
Beta strandi60 – 656Combined sources
Beta strandi68 – 703Combined sources
Helixi71 – 744Combined sources
Helixi80 – 856Combined sources
Beta strandi90 – 945Combined sources
Helixi96 – 1016Combined sources
Helixi106 – 11914Combined sources
Beta strandi122 – 1276Combined sources
Helixi131 – 1355Combined sources
Helixi139 – 15214Combined sources
Helixi156 – 1616Combined sources
Beta strandi162 – 1676Combined sources
Helixi169 – 1713Combined sources
Beta strandi172 – 1754Combined sources
Helixi180 – 19718Combined sources
Helixi200 – 2056Combined sources
Beta strandi208 – 2136Combined sources
Turni216 – 2183Combined sources
Helixi219 – 2235Combined sources
Beta strandi224 – 2274Combined sources
Beta strandi230 – 2345Combined sources
Helixi235 – 2384Combined sources
Helixi242 – 2476Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AG1X-ray2.36O/T1-250[»]
1DKWX-ray2.65A/B2-250[»]
1IIGX-ray2.60A/B1-250[»]
1IIHX-ray2.20A/B1-250[»]
1KV5X-ray1.65A/B1-250[»]
1ML1X-ray2.60A/C/E/G/I/K1-250[»]
1MSSX-ray2.40A/B1-250[»]
1MTMmodel-A1-250[»]
1TPDX-ray2.10A/B1-250[»]
1TPEX-ray2.10A1-250[»]
1TPFX-ray1.80A/B1-250[»]
1TRDX-ray2.50A/B1-250[»]
1TRIX-ray2.40A1-250[»]
1TSIX-ray2.84A/B1-250[»]
1TTIX-ray2.40A1-250[»]
1TTJX-ray2.40A1-250[»]
2J24X-ray2.10A/B1-250[»]
2J27X-ray1.15A/B1-250[»]
2V0TX-ray2.20A/B/C/D/E/F/G/H1-250[»]
2V2CX-ray1.89A1-250[»]
2V2DX-ray2.30A1-250[»]
2V2HX-ray1.18A/B/C1-250[»]
2V5LX-ray2.40A/B1-250[»]
2VEIX-ray1.89A/B/C2-250[»]
2VEKX-ray1.60A/B2-250[»]
2VELX-ray2.30A/B2-250[»]
2VEMX-ray2.20A/B2-250[»]
2VENX-ray2.00A/B2-250[»]
2WSQX-ray2.10A/B/C/D2-67[»]
A/B/C/D84-250[»]
2WSRX-ray1.65A2-67[»]
A84-250[»]
2X16X-ray2.13A/B2-250[»]
2X1RX-ray1.98A/B2-250[»]
2X1SX-ray1.93A/B2-250[»]
2X1TX-ray1.83A/B2-250[»]
2X1UX-ray1.84A/B2-250[»]
2X2GX-ray1.90A/B2-250[»]
2Y6ZX-ray2.60A1-250[»]
2Y70X-ray2.30A/B/C/D1-250[»]
3Q37X-ray1.65A/B/C/D2-249[»]
3TIMX-ray2.80A/B1-250[»]
4JEQX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L1-250[»]
4PC8X-ray1.55A1-250[»]
4PCFX-ray2.71A/B/C1-250[»]
4TIMX-ray2.40A/B1-250[»]
5I3FX-ray1.72A/B/C/D1-250[»]
5I3GX-ray1.96A/B/C/D1-250[»]
5I3HX-ray2.25A/B1-250[»]
5I3IX-ray2.20A/B/C/D1-250[»]
5I3JX-ray1.80A/B1-250[»]
5I3KX-ray2.21A/B/C/D1-250[»]
5TIMX-ray1.83A/B1-250[»]
6TIMX-ray2.20A/B1-250[»]
ProteinModelPortaliP04789.
SMRiP04789. Positions 1-250.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04789.

Family & Domainsi

Sequence similaritiesi

Belongs to the triosephosphate isomerase family.Curated

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.

P04789-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKPQPIAAA NWKCNGSQQS LSELIDLFNS TSINHDVQCV VASTFVHLAM
60 70 80 90 100
TKERLSHPKF VIAAQNAIAK SGAFTGEVSL PILKDFGVNW IVLGHSERRA
110 120 130 140 150
YYGETNEIVA DKVAAAVASG FMVIACIGET LQERESGRTA VVVLTQIAAI
160 170 180 190 200
AKKLKKADWA KVVIAYEPVW AIGTGKVATP QQAQEAHALI RSWVSSKIGA
210 220 230 240 250
DVAGELRILY GGSVNGKNAR TLYQQRDVNG FLVGGASLKP EFVDIIKATQ
Length:250
Mass (Da):26,835
Last modified:February 1, 1995 - v2
Checksum:i189D7A00632040FE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03921 Genomic DNA. Translation: CAA27559.1.

Genome annotation databases

GeneDBiTb927.11.5520:pep.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03921 Genomic DNA. Translation: CAA27559.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AG1X-ray2.36O/T1-250[»]
1DKWX-ray2.65A/B2-250[»]
1IIGX-ray2.60A/B1-250[»]
1IIHX-ray2.20A/B1-250[»]
1KV5X-ray1.65A/B1-250[»]
1ML1X-ray2.60A/C/E/G/I/K1-250[»]
1MSSX-ray2.40A/B1-250[»]
1MTMmodel-A1-250[»]
1TPDX-ray2.10A/B1-250[»]
1TPEX-ray2.10A1-250[»]
1TPFX-ray1.80A/B1-250[»]
1TRDX-ray2.50A/B1-250[»]
1TRIX-ray2.40A1-250[»]
1TSIX-ray2.84A/B1-250[»]
1TTIX-ray2.40A1-250[»]
1TTJX-ray2.40A1-250[»]
2J24X-ray2.10A/B1-250[»]
2J27X-ray1.15A/B1-250[»]
2V0TX-ray2.20A/B/C/D/E/F/G/H1-250[»]
2V2CX-ray1.89A1-250[»]
2V2DX-ray2.30A1-250[»]
2V2HX-ray1.18A/B/C1-250[»]
2V5LX-ray2.40A/B1-250[»]
2VEIX-ray1.89A/B/C2-250[»]
2VEKX-ray1.60A/B2-250[»]
2VELX-ray2.30A/B2-250[»]
2VEMX-ray2.20A/B2-250[»]
2VENX-ray2.00A/B2-250[»]
2WSQX-ray2.10A/B/C/D2-67[»]
A/B/C/D84-250[»]
2WSRX-ray1.65A2-67[»]
A84-250[»]
2X16X-ray2.13A/B2-250[»]
2X1RX-ray1.98A/B2-250[»]
2X1SX-ray1.93A/B2-250[»]
2X1TX-ray1.83A/B2-250[»]
2X1UX-ray1.84A/B2-250[»]
2X2GX-ray1.90A/B2-250[»]
2Y6ZX-ray2.60A1-250[»]
2Y70X-ray2.30A/B/C/D1-250[»]
3Q37X-ray1.65A/B/C/D2-249[»]
3TIMX-ray2.80A/B1-250[»]
4JEQX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L1-250[»]
4PC8X-ray1.55A1-250[»]
4PCFX-ray2.71A/B/C1-250[»]
4TIMX-ray2.40A/B1-250[»]
5I3FX-ray1.72A/B/C/D1-250[»]
5I3GX-ray1.96A/B/C/D1-250[»]
5I3HX-ray2.25A/B1-250[»]
5I3IX-ray2.20A/B/C/D1-250[»]
5I3JX-ray1.80A/B1-250[»]
5I3KX-ray2.21A/B/C/D1-250[»]
5TIMX-ray1.83A/B1-250[»]
6TIMX-ray2.20A/B1-250[»]
ProteinModelPortaliP04789.
SMRiP04789. Positions 1-250.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP04789.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneDBiTb927.11.5520:pep.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00189.
UPA00138.
BRENDAi5.3.1.1. 6519.
SABIO-RKP04789.

Miscellaneous databases

EvolutionaryTraceiP04789.

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. "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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.

Entry informationi

Entry nameiTPIS_TRYBB
AccessioniPrimary (citable) accession number: P04789
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: February 1, 1995
Last modified: July 6, 2016
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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 (PubMed:3015595).1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing

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

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 one 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.