{PDOC00155}
{PS00171; TIM_1}
{PS51440; TIM_2}
{BEGIN}
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* Triosephosphate isomerase (TIM) family signature and profile *
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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 beta/alpha 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.

-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.

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

-Last update: March 2009 / Text revised; profile added.

[ 1] Lolis E., Alber T., Davenport R.C., Rose D., Hartman F.C., Petsko G.A.
     "Structure of yeast triosephosphate isomerase at 1.9-A resolution."
     Biochemistry 29:6609-6618(1990).
     PubMed=2204417
[ 2] Knowles J.R.
     "Enzyme catalysis: not different, just better."
     Nature 350:121-124(1991).
     PubMed=2005961; DOI=10.1038/350121a0
[ 3] Jogl G., Rozovsky S., McDermott A.E., 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. 100:50-55(2003).
     PubMed=12509510; DOI=10.1073/pnas.0233793100
[ 4] Nagano N., Orengo C.A., Thornton J.M.
     "One fold with many functions: the evolutionary relationships between
     TIM barrel families based on their sequences, structures and
     functions."
     J. Mol. Biol. 321:741-765(2002).
     PubMed=12206759

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