Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Triosephosphate isomerase, glycosomal

Gene
N/A
Organism
Trypanosoma cruzi
Status
Reviewed-Annotation score: Annotation score: 3 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 (TCSYLVIO_001494), Triosephosphate isomerase, 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 sitei12 – 121SubstrateBy similarity
Binding sitei14 – 141SubstrateBy similarity
Active sitei96 – 961ElectrophileBy similarity
Active sitei168 – 1681Proton acceptorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Gluconeogenesis, Glycolysis, Pentose shunt

Enzyme and pathway databases

BRENDAi5.3.1.1. 6524.
SABIO-RKP52270.
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 cruzi
Taxonomic identifieri5693 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Glycosome, Peroxisome

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5834.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 251251Triosephosphate isomerase, glycosomalPRO_0000090143Add
BLAST

Proteomic databases

PaxDbiP52270.
PRIDEiP52270.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi353153.XP_818253.1.

Chemistry

BindingDBiP52270.

Structurei

Secondary structure

1
251
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125Combined sources
Helixi19 – 3113Combined sources
Beta strandi39 – 435Combined sources
Helixi46 – 483Combined sources
Helixi49 – 557Combined sources
Beta strandi61 – 666Combined sources
Beta strandi69 – 713Combined sources
Helixi81 – 877Combined sources
Beta strandi91 – 955Combined sources
Helixi97 – 1026Combined sources
Helixi107 – 11913Combined sources
Beta strandi123 – 1286Combined sources
Helixi132 – 1365Combined sources
Helixi140 – 15213Combined sources
Helixi157 – 1626Combined sources
Beta strandi163 – 1675Combined sources
Helixi170 – 1723Combined sources
Beta strandi173 – 1764Combined sources
Helixi181 – 19919Combined sources
Helixi201 – 2066Combined sources
Beta strandi208 – 2114Combined sources
Turni217 – 2193Combined sources
Helixi220 – 2245Combined sources
Beta strandi231 – 2344Combined sources
Helixi236 – 2394Combined sources
Helixi243 – 2486Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CI1X-ray2.00A/B1-251[»]
1SUXX-ray2.00A/B1-251[»]
1TCDX-ray1.83A/B3-251[»]
2OMAX-ray2.15A/B2-251[»]
2V5BX-ray2.00A84-251[»]
3Q37X-ray1.65A/B/C/D37-92[»]
A/B/C/D121-251[»]
4HHPX-ray1.50A/B1-251[»]
ProteinModelPortaliP52270.
SMRiP52270. Positions 2-251.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52270.

Family & Domainsi

Sequence similaritiesi

Belongs to the triosephosphate isomerase family.Curated

Phylogenomic databases

eggNOGiKOG1643. Eukaryota.
COG0149. LUCA.

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.

P52270-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASKPQPIAA ANWKCNGSES LLVPLIETLN AATFDHDVQC VVAPTFLHIP
60 70 80 90 100
MTKARLTNPK FQIAAQNAIT RSGAFTGEVS LQILKDYGIS WVVLGHSERR
110 120 130 140 150
LYYGETNEIV AEKVAQACAA GFHVIVCVGE TNEEREAGRT AAVVLTQLAA
160 170 180 190 200
VAQKLSKEAW SRVVIAYEPV WAIGTGKVAT PQQAQEVHEL LRRWVRSKLG
210 220 230 240 250
TDIAAQLRIL YGGSVTAKNA RTLYQMRDIN GFLVGGASLK PEFVEIIEAT

K
Length:251
Mass (Da):27,329
Last modified:October 1, 1996 - v1
Checksum:i03010B66586C186D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53867 Genomic DNA. Translation: AAB58349.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53867 Genomic DNA. Translation: AAB58349.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CI1X-ray2.00A/B1-251[»]
1SUXX-ray2.00A/B1-251[»]
1TCDX-ray1.83A/B3-251[»]
2OMAX-ray2.15A/B2-251[»]
2V5BX-ray2.00A84-251[»]
3Q37X-ray1.65A/B/C/D37-92[»]
A/B/C/D121-251[»]
4HHPX-ray1.50A/B1-251[»]
ProteinModelPortaliP52270.
SMRiP52270. Positions 2-251.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi353153.XP_818253.1.

Chemistry

BindingDBiP52270.
ChEMBLiCHEMBL5834.

Proteomic databases

PaxDbiP52270.
PRIDEiP52270.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1643. Eukaryota.
COG0149. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00189.
UPA00138.
BRENDAi5.3.1.1. 6524.
SABIO-RKP52270.

Miscellaneous databases

EvolutionaryTraceiP52270.

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. "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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS), HOMODIMERIZATION.
    Strain: Ninoa.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), HOMODIMERIZATION.
    Strain: Ninoa.

Entry informationi

Entry nameiTPIS_TRYCR
AccessioniPrimary (citable) accession number: P52270
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 11, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

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.