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Triosephosphate isomerase (EC 5.3.1.1) (TIM) [1] is the glycolytic enzyme that catalyzes 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 and a histidine residue are involved in the catalytic mechanism [2,3].

The tertiary structure of TIM has eight β/α motifs folded into a barrel structure (see <PDB:1NEY>). 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 strongly conserved in all known TIM's and can be used as a signature pattern for this type of enzyme. We also developed a profile that covers the entire TIM structure.

March 2009 / Text revised; profile added.

PROSITE methods (with tools and information) covered by this documentation:

TIM_2, PS51440; Triosephosphate isomerase (TIM) family profile  (MATRIX)

Sequences known to belong to this class detected by the profile: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Domain architecture view of Swiss-Prot proteins matching PS51440 • Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS51440 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS51440 • Scan Swiss-Prot/TrEMBL entries against PS51440 • view ligand binding statistics

Matching PDB structures: 1AG1 1AMK 1AW1 1AW2 ... [ALL]

TIM_1, PS00171; Triosephosphate isomerase active site  (PATTERN)

Consensus pattern: [AVG]-[YLV]-E-P-[LIVMEPKST]-[WYEAS]-[SAL]-[IV]-[GN]-[TEKDVS]-[GKNAD] E is the active site residue Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00171 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00171 • Scan Swiss-Prot/TrEMBL entries against PS00171 • view ligand binding statistics

Matching PDB structures: 1AG1 1AMK 1AW1 1AW2 ... [ALL]

1	Authors	Lolis E., Alber T., Davenport R.C., Rose D., Hartman F.C., Petsko G.A.
	Title	Structure of yeast triosephosphate isomerase at 1.9-A resolution.
	Source	Biochemistry 29:6609-6618(1990).
	PubMed ID	2204417

2	Authors	Knowles J.R.
	Title	Enzyme catalysis: not different, just better.
	Source	Nature 350:121-124(1991).
	PubMed ID	2005961
	DOI	10.1038/350121a0

3	Authors	Jogl G., Rozovsky S., McDermott A.E., Tong L.
	Title	Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution.
	Source	Proc. Natl. Acad. Sci. U.S.A. 100:50-55(2003).
	PubMed ID	12509510
	DOI	10.1073/pnas.0233793100

4	Authors	Nagano N., Orengo C.A., Thornton J.M.
	Title	One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions.
	Source	J. Mol. Biol. 321:741-765(2002).
	PubMed ID	12206759

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