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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)DescriptionActionsGraphical viewLength
Binding sitei11Substrate1
Binding sitei13Substrate1
Active sitei95Electrophile1
Active sitei167Proton acceptor1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000901421 – 250Triosephosphate isomerase, glycosomalAdd BLAST250

Proteomic databases

PRIDEiP04789.

Interactioni

Subunit structurei

Homodimer.3 Publications

Structurei

Secondary structure

1250
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 11Combined sources5
Beta strandi14 – 16Combined sources3
Helixi18 – 29Combined sources12
Beta strandi38 – 42Combined sources5
Helixi45 – 47Combined sources3
Helixi48 – 54Combined sources7
Beta strandi60 – 65Combined sources6
Beta strandi68 – 70Combined sources3
Helixi71 – 74Combined sources4
Helixi80 – 85Combined sources6
Beta strandi90 – 94Combined sources5
Helixi96 – 101Combined sources6
Helixi106 – 119Combined sources14
Beta strandi122 – 127Combined sources6
Helixi131 – 135Combined sources5
Helixi139 – 152Combined sources14
Helixi156 – 161Combined sources6
Beta strandi162 – 167Combined sources6
Helixi169 – 171Combined sources3
Beta strandi172 – 175Combined sources4
Helixi180 – 197Combined sources18
Helixi200 – 205Combined sources6
Beta strandi208 – 213Combined sources6
Turni216 – 218Combined sources3
Helixi219 – 223Combined sources5
Beta strandi224 – 227Combined sources4
Beta strandi230 – 234Combined sources5
Helixi235 – 238Combined sources4
Helixi242 – 247Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04789.

Family & Domainsi

Sequence similaritiesi

Belongs to the triosephosphate isomerase family.Curated

Family and domain databases

CDDicd00311. TIM. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00147_B. TIM_B. 1 hit.
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
PDB 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.
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

CDDicd00311. TIM. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00147_B. TIM_B. 1 hit.
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...

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: November 2, 2016
This is version 133 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.