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InterPro: IPR000652 Triosephosphate isomerase

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UniProtKB

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3445 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
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Accession

IPR000652 Triosephosphate_isomerase

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00121	TIM	3427
PROSITE profile	PS51440	TIM_2	3434
PANTHER	PTHR21139	Triophos_ismrse	3195
SuperFamily	SSF51351	Triophos_ismrse	3405
TIGRFAMs	TIGR00419	tim	2509
Signatures in BioMart

InterPro Relationships Help

Contains

IPR013785 Aldolase-type TIM barrel
IPR020861 Triosephosphate isomerase, active site

GO Term annotation Help

Process

GO:0008152 metabolic process

Function

GO:0004807 triose-phosphate isomerase activity

InterPro annotation

Entry Details in BioMart

Abstract

Triosephosphate isomerase (EC:5.3.1.1) (TIM) [1] is the glycolytic enzyme that catalyses the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. TIM plays an important role in several metabolic pathways and is essential for efficient energy production. It is present in eukaryotes as well as in prokaryotes. TIM is a dimer of identical subunits, each of which is made up of about 250 amino-acid residues. A glutamic acid residue is involved in the catalytic mechanism [2, 3].

The tertiary structure of TIM has eight beta/alpha motifs folded into a barrel structure. The TIM barrel fold occurs ubiquitously and is found in numerous other enzymes that can be involved in energy metabolism, macromolecule metabolism, or small molecule metabolism [4].

The sequence around the active site residue is perfectly conserved in all known TIM's. Deficiencies in TIM are associated with haemolytic anaemia coupled with a progressive, severe neurological disorder [5].

Structural links Help

PDB - click here

SCOP: c.1.1.1

CATH: 3.20.20.70

Database links Help

PDBe-motif: PS00171

Enzyme: EC:5.3.1.1

PROSITE doc: PDOC00155

PANDIT: PF00121

Blocks: IPB000652

Pfam Clan: CL0036.20

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000652

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P00942 Triosephosphate isomerase

P17751 Triosephosphate isomerase

P29613 Triosephosphate isomerase

P60174 Triosephosphate isomerase

Q10657 Triosephosphate isomerase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR020861	Triosephosphate isomerase, active site
IPR013785	Aldolase-type TIM barrel
IPR000652	Triosephosphate isomerase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Lolis E, Alber T, Davenport RC, Rose D, Hartman FC, Petsko GA. Structure of yeast triosephosphate isomerase at 1.9-A resolution. Biochemistry 29 6609-18 1990 [PubMed: 2204417] http://dx.doi.org/10.1021/bi00480a009
2.	Knowles JR. Enzyme catalysis: not different, just better. Nature 350 121-4 1991 [PubMed: 2005961] http://dx.doi.org/10.1038/350121a0
3.	Jogl G, Rozovsky S, McDermott AE, Tong L. Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution. Proc. Natl. Acad. Sci. U.S.A. 100 50-5 2003 [PubMed: 12509510] http://dx.doi.org/10.1073/pnas.0233793100
4.	Nagano N, Orengo CA, Thornton JM. One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions. J. Mol. Biol. 321 741-65 2002 [PubMed: 12206759] http://dx.doi.org/10.1016/S0022-2836(02)00649-6
5.	Olah J, Orosz F, Keseru GM, Kovari Z, Kovacs J, Hollan S, Ovadi J. Triosephosphate isomerase deficiency: a neurodegenerative misfolding disease. Biochem. Soc. Trans. 30 30-8 2002 [PubMed: 12023819] http://dx.doi.org/10.1042/0300-5127:0300030

Additional Reading Open in usermanual
	Gayathri P, Banerjee M, Vijayalakshmi A, Azeez S, Balaram H, Balaram P, Murthy MR. Structure of triosephosphate isomerase (TIM) from Methanocaldococcus jannaschii. Acta Crystallogr. D Biol. Crystallogr. 63 2007 206-20 [PubMed: 17242514] http://dx.doi.org/10.1107/S0907444906046488
	Alahuhta M, Salin M, Casteleijn MG, Kemmer C, El-Sayed I, Augustyns K, Neubauer P, Wierenga RK. Structure-based protein engineering efforts with a monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties. Protein Eng. Des. Sel. 21 2008 257-66 [PubMed: 18239072] http://dx.doi.org/10.1093/protein/gzn002
	Olivares-Illana V, Rodriguez-Romero A, Becker I, Berzunza M, Garcia J, Perez-Montfort R, Cabrera N, Lopez-Calahorra F, de Gomez-Puyou MT, Gomez-Puyou A. Perturbation of the Dimer Interface of Triosephosphate Isomerase and its Effect on Trypanosoma cruzi. PLoS Negl Trop Dis 1 2007 e1 [PubMed: 17989778] http://dx.doi.org/10.1371/journal.pntd.0000001
	Reyes-Vivas H, Diaz A, Peon J, Mendoza-Hernandez G, Hernandez-Alcantara G, De la Mora-De la Mora I, Enriquez-Flores S, Dominguez-Ramirez L, Lopez-Velazquez G. Disulfide bridges in the mesophilic triosephosphate isomerase from Giardia lamblia are related to oligomerization and activity. J. Mol. Biol. 365 2007 752-63 [PubMed: 17095008] http://dx.doi.org/10.1016/j.jmb.2006.10.053
	Alahuhta M, Casteleijn MG, Neubauer P, Wierenga RK. Structural studies show that the A178L mutation in the C-terminal hinge of the catalytic loop-6 of triosephosphate isomerase (TIM) induces a closed-like conformation in dimeric and monomeric TIM. Acta Crystallogr. D Biol. Crystallogr. 64 2008 178-88 [PubMed: 18219118] http://dx.doi.org/10.1107/S0907444907059021

InterPro 23.1